Multivalent presentation of cationic peptides on supramolecular nanofibers for antimicrobial activity

Date
2017
Advisor
Instructor
Source Title
Molecular Pharmaceutics
Print ISSN
1543-8384
Electronic ISSN
Publisher
American Chemical Society
Volume
14
Issue
11
Pages
3660 - 3668
Language
English
Type
Article
Journal Title
Journal ISSN
Volume Title
Abstract

Noncovalent and electrostatic interactions facilitate the formation of complex networks through molecular self-assembly in biomolecules such as proteins and glycosaminoglycans. Self-assembling peptide amphiphiles (PA) are a group of molecules that can form nanofibrous structures and may contain bioactive epitopes to interact specifically with target molecules. Here, we report the presentation of cationic peptide sequences on supramolecular nanofibers formed by self-assembling peptide amphiphiles for cooperative enhanced antibacterial activity. Antibacterial properties of self-assembled peptide nanofibers were significantly higher than soluble peptide molecules with identical amino acid sequences, suggesting that the tandem presentation of bioactive epitopes is important for designing new materials for bactericidal activity. In addition, bacteria were observed to accumulate more rapidly on peptide nanofibers compared to soluble peptides, which may further enhance antibacterial activity by increasing the number of peptide molecules interacting with the bacterial membrane. The cationic peptide amphiphile nanofibers were observed to attach to bacterial membranes and disrupt their integrity. These results demonstrate that short cationic peptides show a significant improvement in antibacterial activity when presented in the nanofiber form.

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Other identifiers
Book Title
Keywords
Antibacterial peptide, Cationic peptide, Multivalent presentation, Peptide nanofiber, Amphophile, Antimicrobial cationic peptide, Epitope, Glycosaminoglycan, Nanofiber, Amino acid sequence, Antibacterial activity, Antimicrobial activity, Article, Bacillus subtilis, Bacterial membrane, Bactericidal activity, Beta sheet, Complex formation, Controlled study, Escherichia coli, Human, Human cell, Minimum inhibitory concentration, Molecular interaction, Nonhuman, Priority journal, Supramolecular chemistry
Citation
Published Version (Please cite this version)