Peptide-coating combating antimicrobial contaminations: a review of covalent immobilization strategies for industrial applications
Source abstract
Abstract
Abstract Many corrosion problems are caused by the presence of microorganisms, so-called microbiologically influenced corrosion (MIC). A major representative of MIC-causing bacteria includes the group of sulfate-reducing bacteria (SRB), which accumulate in biofilms on the surface. Removal of biofilm inhabiting bacteria is much more complex compared to planktonic cell removal, in particular, based on the formation of an extracellular polymeric substance matrix (EPS layer). Current control strategies mainly involve the use of biocides. The development of resistance is a major problem caused by the limited number of suitable biocides and their frequent use. A consequence is a requirement of even elevated concentrations, which in worst-case scenarios results in a complete loss of efficacy. Recently, the use of antimicrobial peptides (AMPs) especially in the field of medical devices has been distinguished, including the coating of implants with AMPs for retarding or even completely preventing biofilm formation. Transferring AMPs to technical applications as MIC controlling agents offers high potential, therefore. However, based on open circuits, e.g. MIC on ship trunks or in wastewater pipes, immobilization of AMPs on surfaces is quite important, while keeping the AMPs active. This article presents various immobilization strategies established for this purpose, with a special focus on covalent AMP immobilization on metal surfaces. Graphical abstract
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Research context
OpenAlex topics: Antimicrobial Peptides and Activities · Antimicrobial agents and applications · Bacterial biofilms and quorum sensing
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
References (100+)
Show source-provided references
1. Flemming HC (1994) Microbial deterioration of materials—fundamentals: economical and technical overview. Mikrobielle Werkstoffzerstoerung—Grundlagen: Oekonomisch-technischer Ueberblick. Werkstoffe und Korrosion (Germany) 45:110.1002/maco.19940450105 ↗
2. Jacobson GA (2007) Corrosion at Purdhoe Bay: a lesson on the line. Mater Perform 46(8):26–32
3. Dou W, Xu D, Gu T (2021) Biocorrosion caused by microbial biofilms is ubiquitous around us. Microb Biotechnol 14:803–805. https://doi.org/10.1111/1751-7915.1369010.1111/1751-7915.13690 ↗
4. Javaherdashti R (1999) A review of some characteristics of MIC caused by sulfate-reducing bacteria: past, present and future. Anti-Corrosion Meth Mater 46:173–180. https://doi.org/10.1108/0003559991027314210.1108/00035599910273142 ↗
5. Mercer AD (1983) Microbial corrosion: proceedings of the conference sponsored and organized jointly by the National Physical Laboratory and the Metals Society and held at NPL Teddington on 8–10 March 1983. Metals Society, London
6. Herisson J, van Hullebusch ED, Moletta-Denat M, Taquet P, Chaussadent T (2013) Toward an accelerated biodeterioration test to understand the behavior of Portland and calcium aluminate cementitious materials in sewer networks. Int Biodeterior Biodegrad 84:236–243. https://doi.org/10.1016/j.ibiod.2012.03.00710.1016/j.ibiod.2012.03.007 ↗
7. Singh AK (2020) Industrial cases of microbial induced corrosion. In: Singh AK, D’Silva (eds) Microbially induced corrosion and its mitigation. [S.l.]. Springer Nature, pp 81–106. https://doi.org/10.1007/978-981-15-8019-2_510.1007/978-981-15-8019-2_5 ↗
8. Unsal T, Wang D, Kumseranee S, Punpruk S, Gu T (2021) D-Tyrosine enhancement of microbiocide mitigation of carbon steel corrosion by a sulfate reducing bacterium biofilm. World J Microbiol Biotechnol 37:103. https://doi.org/10.1007/s11274-021-03072-910.1007/s11274-021-03072-9 ↗
9. Zhang P, Xu D, Li Y, Yang K, Gu T (2015) Electron mediators accelerate the microbiologically influenced corrosion of 304 stainless steel by the Desulfovibrio vulgaris biofilm. Bioelectrochemistry 101:14–21. https://doi.org/10.1016/j.bioelechem.2014.06.01010.1016/j.bioelechem.2014.06.010 ↗
10. Dai X, Wang H, Ju L-K, Cheng G, Cong H, Newby BZ (2016) Corrosion of aluminum alloy 2024 caused by Aspergillus niger. Int Biodeterior Biodegradation 115:1–10. https://doi.org/10.1016/j.ibiod.2016.07.00910.1016/j.ibiod.2016.07.009 ↗
11. Wang D, Liu J, Jia R, Dou W, Kumseranee S, Punpruk S et al (2020) Distinguishing two different microbiologically influenced corrosion (MIC) mechanisms using an electron mediator and hydrogen evolution detection. Corr Sci 177:108993. https://doi.org/10.1016/j.corsci.2020.10899310.1016/j.corsci.2020.108993 ↗
12. Ahmadkhaniha D, Järvenpää A, Jaskari M, Sohi MH, Zarei-Hanzaki A, Fedel M et al (2016) Microstructural modification of pure Mg for improving mechanical and biocorrosion properties. J Mech Behav Biomed Mater 61:360–370. https://doi.org/10.1016/j.jmbbm.2016.04.01510.1016/j.jmbbm.2016.04.015 ↗
13. Ilhan-Sungur E, Unsal-Istek T, Cansever N (2015) Microbiologically influenced corrosion of galvanized steel by Desulfovibrio sp. and Desulfosporosinus sp. in the presence of Ag–Cu ions. Mater Chem Phys 162:839–851. https://doi.org/10.1016/j.matchemphys.2015.07.01210.1016/j.matchemphys.2015.07.012 ↗
14. Saleem Khan M, Li Z, Yang K, Xu D, Yang C, Liu D et al (2019) Microbiologically influenced corrosion of titanium caused by aerobic marine bacterium Pseudomonas aeruginosa. J Mater Sci Technol 35:216–222. https://doi.org/10.1016/j.jmst.2018.08.00110.1016/j.jmst.2018.08.001 ↗
15. Jia R, Unsal T, Xu D, Lekbach Y, Gu T (2019) Microbiologically influenced corrosion and current mitigation strategies: a state of the art review. Int Biodeterior Biodegrad 137:42–58. https://doi.org/10.1016/j.ibiod.2018.11.00710.1016/j.ibiod.2018.11.007 ↗
16. Chugh B, Thakur S, Singh AK (2020) Microbiologically influenced corrosion inhibition in oil and gas industry. In: Saji VS, Umoren SA (eds) Corrosion inhibitors in the oil and gas industry. Wiley-VCH, Weinheim, pp 321–338. https://doi.org/10.1002/9783527822140.ch1310.1002/9783527822140.ch13 ↗
17. Ru Jia DY, Yingchao L, Amir Z, Tingyue G (2017) A novel peptide at a very low concentration enhanced biocide treatment of corrosive biofilms. Paper presented at the CORROSION 2017, New Orleans, Louisiana, USA (Published: March 26 2017)
18. Wen J, Zhao K, Gu T, Raad II (2009) A green biocide enhancer for the treatment of sulfate-reducing bacteria (SRB) biofilms on carbon steel surfaces using glutaraldehyde. Int Biodeterior Biodegrad 63:1102–1106. https://doi.org/10.1016/j.ibiod.2009.09.00710.1016/j.ibiod.2009.09.007 ↗
19. Wen J, Xu D, Gu T, Raad I (2012) A green triple biocide cocktail consisting of a biocide, EDDS and methanol for the mitigation of planktonic and sessile sulfate-reducing bacteria. World J Microbiol Biotechnol 28:431–435. https://doi.org/10.1007/s11274-011-0832-110.1007/s11274-011-0832-1 ↗
20. Givskov M, de Nys R, Manefield M, Gram L, Maximilien R, Eberl L et al (1996) Eukaryotic interference with homoserine lactone-mediated prokaryotic signalling. J Bacteriol 178:6618–6622. https://doi.org/10.1128/jb.178.22.6618-6622.199610.1128/jb.178.22.6618-6622.1996 ↗
21. Scarascia G, Wang T, Hong P-Y (2016) Quorum sensing and the use of quorum quenchers as natural biocides to inhibit sulfate-reducing bacteria. Antibiotics (Basel) 5(4):39. https://doi.org/10.3390/antibiotics504003910.3390/antibiotics5040039 ↗
22. Liu R, Memarzadeh K, Chang B, Zhang Y, Ma Z, Allaker RP et al (2016) Antibacterial effect of copper-bearing titanium alloy (Ti-Cu) against Streptococcus mutans and Porphyromonas gingivalis. Sci Rep 6:29985. https://doi.org/10.1038/srep2998510.1038/srep29985 ↗
23. Gao N, Chen Y, Jiang J (2013) Ag@Fe2O3-GO nanocomposites prepared by a phase transfer method with long-term antibacterial property. ACS Appl Mater Interfaces 5:11307–11314. https://doi.org/10.1021/am403538j10.1021/am403538j ↗
24. Wang G, Li X, Wang Z (2016) APD3: the antimicrobial peptide database as a tool for research and education. Nucleic Acids Res 44:D1087–D1093. https://doi.org/10.1093/nar/gkv127810.1093/nar/gkv1278 ↗
25. Di Luca M, Maccari G, Maisetta G, Batoni G (2015) BaAMPs: the database of biofilm-active antimicrobial peptides. Biofouling 31:193–199. https://doi.org/10.1080/08927014.2015.102134010.1080/08927014.2015.1021340 ↗
26. Brogden KA (2005) Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 3:238–250. https://doi.org/10.1038/nrmicro109810.1038/nrmicro1098 ↗
27. Jayaraman A, Mansfeld FB, Wood TK (1999) Inhibiting sulfate-reducing bacteria in biofilms by expressing the antimicrobial peptides indolicidin and bactenecin. J Ind Microbiol Biotechnol 22:167–175. https://doi.org/10.1038/sj.jim.290062710.1038/sj.jim.2900627 ↗
28. Trepos R, Cervin G, Pile C, Pavia H, Hellio C, Svenson J (2015) Evaluation of cationic micropeptides derived from the innate immune system as inhibitors of marine biofouling. Biofouling 31:393–403. https://doi.org/10.1080/08927014.2015.104823810.1080/08927014.2015.1048238 ↗
29. Herzberg M, Berglin M, Eliahu S, Bodin L, Agrenius K, Zlotkin A, Svenson J (2021) Efficient prevention of marine biofilm formation employing a surface-grafted repellent marine peptide. ACS Appl Bio Mater 4:3360–3373. https://doi.org/10.1021/acsabm.0c0167210.1021/acsabm.0c01672 ↗
30. Kazemzadeh-Narbat M, Cheng H, Chabok R, Alvarez MM, La Fuente-Nunez C de, Phillips KS, Khademhosseini A (2021) Strategies for antimicrobial peptide coatings on medical devices: a review and regulatory science perspective. Crit Rev Biotechnol 41:94–120. https://doi.org/10.1080/07388551.2020.182881010.1080/07388551.2020.1828810 ↗
31. Andrea A, Molchanova N, Jenssen H (2018) Antibiofilm peptides and peptidomimetics with focus on surface immobilization. Biomolecules 8(2):27. https://doi.org/10.3390/biom802002710.3390/biom8020027 ↗
32. Siedenbiedel F, Tiller JC (2012) Antimicrobial polymers in solution and on surfaces: overview and functional principles. Polymers 4:46–71. https://doi.org/10.3390/polym401004610.3390/polym4010046 ↗
33. Chen J, Shi X, Zhu Y, Chen Y, Gao M, Gao H et al (2020) On-demand storage and release of antimicrobial peptides using Pandora’s box-like nanotubes gated with a bacterial infection-responsive polymer. Theranostics 10:109–122. https://doi.org/10.7150/thno.3838810.7150/thno.38388 ↗
34. Zhang T, Wei Q, Zhou H, Zhou W, Fan D, Lin X et al (2020) Sustainable release of vancomycin from micro-arc oxidised 3D-printed porous Ti6Al4V for treating methicillin-resistant Staphylococcus aureus bone infection and enhancing osteogenesis in a rabbit tibia osteomyelitis model. Biomater Sci 8:3106–3115. https://doi.org/10.1039/c9bm01968e10.1039/c9bm01968e ↗
35. Kelson AB, Carnevali M, Truong-Le V (2013) Gallium-based anti-infectives: targeting microbial iron-uptake mechanisms. Curr Opin Pharmacol 13:707–716. https://doi.org/10.1016/j.coph.2013.07.00110.1016/j.coph.2013.07.001 ↗
36. Shirai T, Shimizu T, Ohtani K, Zen Y, Takaya M, Tsuchiya H (2011) Antibacterial iodine-supported titanium implants. Acta Biomater 7:1928–1933. https://doi.org/10.1016/j.actbio.2010.11.03610.1016/j.actbio.2010.11.036 ↗
37. Rodríguez López AdL, Lee M-R, Ortiz BJ, Gastfriend BD, Whitehead R, Lynn DM, Palecek SP (2019) Preventing S. aureus biofilm formation on titanium surfaces by the release of antimicrobial β-peptides from polyelectrolyte multilayers. Acta Biomaterialia 93:50–62. https://doi.org/10.1016/j.actbio.2019.02.04710.1016/j.actbio.2019.02.047 ↗
38. Kord Forooshani P, Lee BP (2017) Recent approaches in designing bioadhesive materials inspired by mussel adhesive protein. J Polym Sci A Polym Chem 55:9–33. https://doi.org/10.1002/pola.2836810.1002/pola.28368 ↗
39. Torres LMFC, Braga NA, Gomes IP, Almeida MT, Santos TL, de Mesquita JP et al (2018) Nanobiostructure of fibrous-like alumina functionalized with an analog of the BP100 peptide: synthesis, characterization and biological applications. Colloids Surf B Biointerfaces 163:275–283. https://doi.org/10.1016/j.colsurfb.2018.01.00110.1016/j.colsurfb.2018.01.001 ↗
40. Torres LMFC, Almeida MT, Santos TL, Marinho LES, de Mesquita JP, Da Silva LM et al (2019) Antimicrobial alumina nanobiostructures of disulfide- and triazole-linked peptides: synthesis, characterization, membrane interactions and biological activity. Colloids Surf B Biointerfaces 177:94–104. https://doi.org/10.1016/j.colsurfb.2019.01.05210.1016/j.colsurfb.2019.01.052 ↗
41. Wang T, Zou C, Wen N, Liu X, Meng Z, Feng S et al (2021) The effect of structural modification of antimicrobial peptides on their antimicrobial activity, hemolytic activity, and plasma stability. J Pept Sci 27:e3306. https://doi.org/10.1002/psc.330610.1002/psc.3306 ↗
42. Gabriel M, Nazmi K, Veerman EC, Nieuw Amerongen AV, Zentner A (2006) Preparation of LL-37-grafted titanium surfaces with bactericidal activity. Bioconjug Chem 17:548–550. https://doi.org/10.1021/bc050091v10.1021/bc050091v ↗
43. Mauchauffé R, Moreno-Couranjou M, Boscher ND, van de Weerdt C, Duwez A-S, Choquet P (2014) Robust bio-inspired antibacterial surfaces based on the covalent binding of peptides on functional atmospheric plasma thin films. J Mater Chem B 2:5168–5177. https://doi.org/10.1039/c4tb00503a10.1039/c4tb00503a ↗
44. Chen G, Zhou M, Chen S, Lv G, Yao J (2009) Nanolayer biofilm coated on magnetic nanoparticles by using a dielectric barrier discharge glow plasma fluidized bed for immobilizing an antimicrobial peptide. Nanotechnology 20:465706. https://doi.org/10.1088/0957-4484/20/46/46570610.1088/0957-4484/20/46/465706 ↗
45. Duday D, Vreuls C, Moreno M, Frache G, Boscher ND, Zocchi G et al (2013) Atmospheric pressure plasma modified surfaces for immobilization of antimicrobial nisin peptides. Surf Coat Technol 218:152–161. https://doi.org/10.1016/j.surfcoat.2012.12.04510.1016/j.surfcoat.2012.12.045 ↗
46. Diaz-Rodriguez S, Chevallier P, Mantovani D (2018) Low-pressure plasma treatment for direct amination of L605 CoCr alloy for the further covalent grafting of molecules. Plasma Process Polym 15:1700214. https://doi.org/10.1002/ppap.20170021410.1002/ppap.201700214 ↗
47. Godoy-Gallardo M, Mas-Moruno C, Yu K, Manero JM, Gil FJ, Kizhakkedathu JN, Rodriguez D (2015) Antibacterial properties of hLf1-11 peptide onto titanium surfaces: a comparison study between silanization and surface initiated polymerization. Biomacromol 16:483–496. https://doi.org/10.1021/bm501528x10.1021/bm501528x ↗
48. Vreuls C, Zocchi G, Thierry B, Garitte G, Griesser SS, Archambeau C et al (2010) Prevention of bacterial biofilms by covalent immobilization of peptides onto plasma polymer functionalized substrates. J Mater Chem 20:8092. https://doi.org/10.1039/c0jm01419b10.1039/c0jm01419b ↗
49. Riordan L, Smith EF, Mills S, Hudson J, Stapley S, Nikoi N-D et al (2019) Directly bonding antimicrobial peptide mimics to steel and the real world applications of these materials. Mater Sci Eng C Mater Biol Appl 102:299–304. https://doi.org/10.1016/j.msec.2019.03.06410.1016/j.msec.2019.03.064 ↗
50. Šimončicová J, Kryštofová S, Medvecká V, Ďurišová K, Kaliňáková B (2019) Technical applications of plasma treatments: current state and perspectives. Appl Microbiol Biotechnol 103:5117–5129. https://doi.org/10.1007/s00253-019-09877-x10.1007/s00253-019-09877-x ↗
51. Mas-Moruno C, Garrido B, Rodriguez D, Ruperez E, Gil FJ (2015) Biofunctionalization strategies on tantalum-based materials for osseointegrative applications. J Mater Sci Mater Med 26:109. https://doi.org/10.1007/s10856-015-5445-z10.1007/s10856-015-5445-z ↗
52. Yildirim E, Choi H, Schulte A, Schönherr H (2021) Synthesis of end group-functionalized PGMA-peptide brush platforms for specific cell attachment by interface-mediated dissociative electron transfer reversible addition-fragmentation chain transfer radical (DET-RAFT) polymerization. Eur Polymer J 148:110370. https://doi.org/10.1016/j.eurpolymj.2021.11037010.1016/j.eurpolymj.2021.110370 ↗
53. Cao P, Yuan C, Xiao J, He X, Bai X (2018) A biofilm resistance surface yielded by grafting of antimicrobial peptides on stainless steel surface. Surf Interface Anal 50:516–521. https://doi.org/10.1002/sia.640610.1002/sia.6406 ↗
54. Alas GR, Agarwal R, Collard DM, García AJ (2017) Peptide-functionalized polyoligo(ethylene glycol) methacrylate brushes on dopamine-coated stainless steel for controlled cell adhesion. Acta Biomater 59:108–116. https://doi.org/10.1016/j.actbio.2017.06.03310.1016/j.actbio.2017.06.033 ↗
55. Swan EEL, Popat KC, Desai TA (2005) Peptide-immobilized nanoporous alumina membranes for enhanced osteoblast adhesion. Biomaterials 26:1969–1976. https://doi.org/10.1016/j.biomaterials.2004.07.00110.1016/j.biomaterials.2004.07.001 ↗
56. Nie B, Long T, Li H, Wang X, Yue B (2017) A comparative analysis of antibacterial properties and inflammatory responses for the KR-12 peptide on titanium and PEGylated titanium surfaces. RSC Adv 7:34321–34330. https://doi.org/10.1039/C7RA05538B10.1039/C7RA05538B ↗
57. Khanjanzadeh H, Behrooz R, Bahramifar N, Pinkl S, Gindl-Altmutter W (2019) Application of surface chemical functionalized cellulose nanocrystals to improve the performance of UF adhesives used in wood based composites—MDF type. Carbohyd Polym 206:11–20. https://doi.org/10.1016/j.carbpol.2018.10.11510.1016/j.carbpol.2018.10.115 ↗
58. Majhi S, Peddiraju VC, Mishra A (2021) Effect of antimicrobial peptide (AMP)–tethered stainless steel surfaces on the bacterial membrane. Mater Today Chem 21:100541. https://doi.org/10.1016/j.mtchem.2021.10054110.1016/j.mtchem.2021.100541 ↗
59. Aditya A, Chattopadhyay S, Gupta N, Alam S, Veedu AP, Pal M et al (2019) ZnO nanoparticles modified with an amphipathic peptide show improved photoprotection in skin. ACS Appl Mater Interfaces 11:56–72. https://doi.org/10.1021/acsami.8b0843110.1021/acsami.8b08431 ↗
60. Cao L, Wang L, Fan L, Xiao W, Lin B, Xu Y et al (2017) RGDC peptide-induced biomimetic calcium phosphate coating formed on AZ31 magnesium alloy. Materials (Basel) 10(4):358. https://doi.org/10.3390/ma1004035810.3390/ma10040358 ↗
61. Pang LQ, Zhong LJ, Zhou HF, Wu XE, Chen XD (2015) Grafting of ionic liquids on stainless steel surface for antibacterial application. Colloids Surf B Biointerfaces 126:162–168. https://doi.org/10.1016/j.colsurfb.2014.12.01810.1016/j.colsurfb.2014.12.018 ↗
62. Bekmurzayeva A, Duncanson WJ, Azevedo HS, Kanayeva D (2018) Surface modification of stainless steel for biomedical applications: Revisiting a century-old material. Mater Sci Eng C Mater Biol Appl 93:1073–1089. https://doi.org/10.1016/j.msec.2018.08.04910.1016/j.msec.2018.08.049 ↗
63. Magalhães S, Alves L, Medronho B, Fonseca AC, Romano A, Coelho JFJ, Norgren M (2019) Brief overview on bio-based adhesives and sealants. Polymers 11(10):1685. https://doi.org/10.3390/polym1110168510.3390/polym11101685 ↗
64. Rosenthal A, Mantz A, Nguyen A, Bittrich E, Schubert E, Schubert M et al (2018) Biofunctionalization of titanium substrates using nanoscale polymer brushes with cell adhesion peptides. J Phys Chem B 122:6543–6550. https://doi.org/10.1021/acs.jpcb.8b0240710.1021/acs.jpcb.8b02407 ↗
65. Hofman AH, van Hees IA, Yang J, Kamperman M (2018) Bioinspired underwater adhesives by using the supramolecular toolbox. Adv Mater 30:e1704640. https://doi.org/10.1002/adma.20170464010.1002/adma.201704640 ↗
66. Lee H, Dellatore SM, Miller WM, Messersmith PB (2007) Mussel-inspired surface chemistry for multifunctional coatings. Science 318:426–430. https://doi.org/10.1126/science.114724110.1126/science.1147241 ↗
67. Jaramillo J, Rodriguez-Oliva I, Abian O, Palomo JM (2020) Specific chemical incorporation of l-DOPA and functionalized l-DOPA-hyaluronic acid in Candida antarctica lipase: creating potential mussel-inspired bioadhesives. SN Appl Sci 2:1–12. https://doi.org/10.1007/s42452-020-03545-w10.1007/s42452-020-03545-w ↗
68. Yang J, Saggiomo V, Velders AH, Cohen Stuart MA, Kamperman M (2016) Reaction pathways in catechol/primary amine mixtures: a window on crosslinking chemistry. PLoS ONE 11:e0166490. https://doi.org/10.1371/journal.pone.016649010.1371/journal.pone.0166490 ↗
69. Cao P, Liu K, Liu X, Sun W, Wu D, Yuan C et al (2020) Antibacterial properties of Magainin II peptide onto 304 stainless steel surfaces: A comparison study of two dopamine modification methods. Colloids Surf B Biointerfaces 194:111198. https://doi.org/10.1016/j.colsurfb.2020.11119810.1016/j.colsurfb.2020.111198 ↗
70. Cao P, Yang Y, Uche FI, Hart SR, Li W-W, Yuan C (2018) Coupling plant-derived cyclotides to metal surfaces: an antibacterial and antibiofilm study. Int J Mol Sci 19(3):793. https://doi.org/10.3390/ijms1903079310.3390/ijms19030793 ↗
71. Cao P, Li W-W, Morris AR, Horrocks PD, Yuan C-Q, Yang Y (2018) Investigation of the antibiofilm capacity of peptide-modified stainless steel. R Soc Open Sci 5:172165. https://doi.org/10.1098/rsos.17216510.1098/rsos.172165 ↗
72. Cao P, Du C, He X, Zhang C, Yuan C (2020) Modification of a derived antimicrobial peptide on steel surface for marine bacterial resistance. Appl Surf Sci 510:145512. https://doi.org/10.1016/j.apsusc.2020.14551210.1016/j.apsusc.2020.145512 ↗
73. Ryu JH, Messersmith PB, Lee H (2018) Polydopamine surface chemistry: a decade of discovery. ACS Appl Mater Interfaces 10:7523–7540. https://doi.org/10.1021/acsami.7b1986510.1021/acsami.7b19865 ↗
74. Levin A, Hakala TA, Schnaider L, Bernardes GJL, Gazit E, Knowles TPJ (2020) Biomimetic peptide self-assembly for functional materials. Nat Rev Chem 4:615–634. https://doi.org/10.1038/s41570-020-0215-y10.1038/s41570-020-0215-y ↗
75. Ulman A (1996) Formation and structure of self-assembled monolayers. Chem Rev 96:1533–1554. https://doi.org/10.1021/cr950235710.1021/cr9502357 ↗
76. Zhang Z, Kou N, Ye W, Wang S, Lu J, Lu Y et al (2021) Construction and characterizations of antibacterial surfaces based on self-assembled monolayer of antimicrobial peptides (Pac-525) derivatives on gold. Coatings 11(9):1014. https://doi.org/10.3390/coatings1109101410.3390/coatings11091014 ↗
77. Humblot V, Yala J-F, Thebault P, Boukerma K, Héquet A, Berjeaud J-M, Pradier C-M (2009) The antibacterial activity of Magainin I immobilized onto mixed thiols self-assembled monolayers. Biomaterials 30:3503–3512. https://doi.org/10.1016/j.biomaterials.2009.03.02510.1016/j.biomaterials.2009.03.025 ↗
78. Brown MA, Cortes-Lobos R, Cox M (2011) Chapter 12—reinventing industrial energy use in a resource-constrained world. In: Sioshansi FP (ed) Energy, sustainability and the environment. Butterworth-Heinemann, Boston, pp 337–366. https://doi.org/10.1016/B978-0-12-385136-9.10012-910.1016/B978-0-12-385136-9.10012-9 ↗
79. Sudha E, Selvam R, Sivaswaroop P, Chandran KPS (2017) Diimide activated coupling of carbon nanotubes with chemically addressable peptide template for biomedical applications. Indian J Chem Technol 67–72
80. Wilke G (1979) Organo transition metal compounds as intermediates in homogeneous catalytic reactions. In: Ishii Y, Hagihara N (eds) Organometallic chemistry: pergamon, pp 677–690. https://doi.org/10.1016/B978-0-08-022035-2.50012-810.1016/B978-0-08-022035-2.50012-8 ↗
81. Takakura A, Beppu K, Nishihara T, Fukui A, Kozeki T, Namazu T et al (2019) Strength of carbon nanotubes depends on their chemical structures. Nat Commun 10:3040. https://doi.org/10.1038/s41467-019-10959-710.1038/s41467-019-10959-7 ↗
82. Poh CK, Shi Z, Tan XW, Liang ZC, Foo XM, Tan HC et al (2011) Cobalt chromium alloy with immobilized BMP peptide for enhanced bone growth. J Orthop Res 29:1424–1430. https://doi.org/10.1002/jor.2140910.1002/jor.21409 ↗
83. Tan HC, Poh CK, Cai Y, Wang W (2013) Anti-fibrosis effect of BMP-7 peptide functionalization on cobalt chromium alloy. J Orthop Res 31:983–990. https://doi.org/10.1002/jor.2231310.1002/jor.22313 ↗
84. Campbell D, Carnell SM, Eden RJ (2013) Applicability of contact angle techniques used in the analysis of contact lenses, part 1: comparative methodologies. Eye Contact Lens 39:254–262. https://doi.org/10.1097/ICL.0b013e31828ca17410.1097/ICL.0b013e31828ca174 ↗
85. Puiu M, Bala C (2016) SPR and SPR imaging: recent trends in developing nanodevices for detection and real-time monitoring of biomolecular events. Sensors (Basel) 16(6):870. https://doi.org/10.3390/s1606087010.3390/s16060870 ↗
86. Nabok AV, Tsargorodskaya A, Hassan AK, Starodub NF (2005) Total internal reflection ellipsometry and SPR detection of low molecular weight environmental toxins. Appl Surf Sci 246:381–386. https://doi.org/10.1016/j.apsusc.2004.11.08410.1016/j.apsusc.2004.11.084 ↗
87. Morent R, de Geyter N, Leys C, Gengembre L, Payen E (2008) Comparison between XPS- and FTIR-analysis of plasma-treated polypropylene film surfaces. Surf Interface Anal 40:597–600. https://doi.org/10.1002/sia.261910.1002/sia.2619 ↗
88. Andrade JD (1985) X-ray photoelectron spectroscopy (XPS). In: Andrade JD (ed) Surface and interfacial aspects of biomedical polymers. Springer US, Boston, MA, pp 105–195. https://doi.org/10.1007/978-1-4684-8610-0_510.1007/978-1-4684-8610-0_5 ↗
89. Zhang X-F, Liu Z-G, Shen W, Gurunathan S (2016) Silver nanoparticles: synthesis, characterization, properties, applications, and therapeutic approaches. Int J Mol Sci 17(9):1534. https://doi.org/10.3390/ijms1709153410.3390/ijms17091534 ↗
90. Klemm D, Stangl M, Peeva A, Hoffmann V, Wetzig K, Eckert J (2008) Analysis of interface impurities in electroplated Cu layers by using GD-OES and TOF-SIMS. Surf Interface Anal 40:418–422. https://doi.org/10.1002/sia.274310.1002/sia.2743 ↗
91. Arenas-Alatorre J, Silva-Velazquez Y, Alva Medina A, Rivera M (2010) Advantages and limitations of OM, SEM, TEM and AFM in the study of ancient decorated pottery. Appl Phys A 98:617–624. https://doi.org/10.1007/s00339-009-5451-410.1007/s00339-009-5451-4 ↗
92. Glover RD, Miller JM, Hutchison JE (2011) Generation of metal nanoparticles from silver and copper objects: nanoparticle dynamics on surfaces and potential sources of nanoparticles in the environment. ACS Nano 5:8950–8957. https://doi.org/10.1021/nn203131910.1021/nn2031319 ↗
93. Dutta D, Kumar N, Willcox MDP (2016) Antimicrobial activity of four cationic peptides immobilised to poly-hydroxyethylmethacrylate. Biofouling 32:429–38. https://doi.org/10.1080/08927014.2015.112953310.1080/08927014.2015.1129533 ↗
94. Kang S-J, Won H-S, Choi W-S, Lee B-J (2009) De novo generation of antimicrobial LK peptides with a single tryptophan at the critical amphipathic interface. J Pept Sci 15:583–588. https://doi.org/10.1002/psc.114910.1002/psc.1149 ↗
95. Béven L, Castano S, Dufourcq J, Wieslander A, Wróblewski H (2003) The antibiotic activity of cationic linear amphipathic peptides: lessons from the action of leucine/lysine copolymers on bacteria of the class Mollicutes. Eur J Biochem 270:2207–2217. https://doi.org/10.1046/j.1432-1033.2003.03587.x10.1046/j.1432-1033.2003.03587.x ↗
96. Carmona G, Rodriguez A, Juarez D, Corzo G, Villegas E (2013) Improved protease stability of the antimicrobial peptide Pin2 substituted with D-amino acids. Protein J 32:456–466. https://doi.org/10.1007/s10930-013-9505-210.1007/s10930-013-9505-2 ↗
97. Lu J, Xu H, Xia J, Ma J, Xu J, Li Y, Feng J (2020) D- and unnatural amino acid substituted antimicrobial peptides with improved proteolytic resistance and their proteolytic degradation characteristics. Front Microbiol 11:563030. https://doi.org/10.3389/fmicb.2020.56303010.3389/fmicb.2020.563030 ↗
98. Haney EF, Barbosa SC, Baquir B, Hancock REW (2019) Influence of non-natural cationic amino acids on the biological activity profile of innate defense regulator peptides. J Med Chem 62:10294–10304. https://doi.org/10.1021/acs.jmedchem.9b0134410.1021/acs.jmedchem.9b01344 ↗
99. Shao C, Zhu Y, Lai Z, Tan P, Shan A (2019) Antimicrobial peptides with protease stability: progress and perspective. Future Med Chem 11:2047–2050. https://doi.org/10.4155/fmc-2019-016710.4155/fmc-2019-0167 ↗
100. Avan I, Hall CD, Katritzky AR (2014) Peptidomimetics via modifications of amino acids and peptide bonds. Chem Soc Rev 43:3575–3594. https://doi.org/10.1039/C3CS60384A10.1039/C3CS60384A ↗