Nanoparticle Assembly and Gelatin Binding Mediated by Triple Helical Collagen Mimetic Peptide
Source abstract
Abstract
Peptide-conjugated nanoparticles (NPs) have promising potential for applications in biosensing, diagnosis, and therapeutics because of their appropriate size, unique self-assembly, and specific substrate-binding properties. However, controlled assembly and selective target binding are difficult to achieve with simple peptides on NP surfaces because high surface energy makes NPs prone to self-aggregate and adhere nonspecifically. Here, we report the self-assembly and gelatin binding properties of collagen mimetic peptide (CMP) conjugated gold NPs (CMP-NPs). We show that the orientation of CMPs displayed on the NP surface can control NP assembly either by promoting or hindering triple helical folding between CMPs of neighboring NPs. We also show that CMP-NPs can specifically bind to denatured collagen by forming triple-helical hybrids between denatured collagen strands and CMPs, demonstrating their potential use for detection and selective removal of gelatin from protein mixtures. CMP conjugated NPs offer a simple and effective method for NP assembly and for targeting denatured collagens with high specificity. Therefore, they may lead to new types of functional nanomaterials for detection and study of denatured collagen associated with diseases characterized by high levels of collagen degradation.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Collagen: Extraction and Characterization · Protein Hydrolysis and Bioactive Peptides · Marine Biology and Environmental Chemistry
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Department of Bioengineering, University of Utah, Salt Lake City, Utah 84112, United States
Institute for Antiviral Research, Utah State University, Logan, Utah 84322, United States
Funding
Congressionally Directed Medical Research Programs · National Institute of Arthritis and Musculoskeletal and Skin Diseases
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