journal article·2021-06-02

Switchable Self-Assembly of Elastin- and Resilin-Based Block Copolypeptides with Converse Phase Transition Behaviors

Aamna Basheer, Shahzaib Shahid, Min Jung Kang, Jae Hee Lee, Jae Sang Lee, Dong Woo Lim

ACS Applied Materials & Interfaces· Volume 13· Issue 21
Publisher page

Abstract

Self-assembly of thermally responsive polypeptides into unique nanostructures offers intriguing attributes including dynamic physical dimensions, biocompatibility, and biodegradability for the smart bio-nanomaterials. As elastin-based polypeptide (EBP) fusion proteins with lower critical solution temperature (LCST) are studied as drug delivery systems, EBP block copolypeptides with the resilin-based polypeptide (RBP) displaying an upper critical solution temperature (UCST) have been of great interest. In this study, we report thermally triggered, dynamic self-assembly of EBP- and RBP-based diblock copolypeptides into switched nanostructures with reversibility under physiological conditions. Molecular DNA clones encoding for the EBP-RBP diblocks at different block length ratios were biosynthesized via recursive directional ligation and overexpressed, followed by nonchromatographic purification by inverse transition cycling. Genetically engineered diblock copolypeptides composed of the EBP with an LCST and the RBP with a UCST showed converse phase transition behaviors with both a distinct LCST and a distinct UCST (LCST < UCST). As temperature increased, three phases of these EBP-RBP diblocks were observed: (1) self-assembled micelles or vesicles below both LCST and UCST, (2) whole aggregates above LCST and below UCST, and (3) reversed micelles above both LCST and UCST. In conclusion, these stimuli-triggered, dynamic protein-based nanostructures are promising for advanced drug delivery systems, regenerative medicine, and biomedical nanotechnology.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Connective tissue disorders research · Silk-based biomaterials and applications · Glycosylation and Glycoproteins Research

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Department of Bionano Engineering and Department of Bionanotechnology, Center for Bionano Intelligence Education and Research, Hanyang University, Ansan 15588, Republic of Korea

Funding

National Research Foundation of Korea

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