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Ultra-low fouling peptide surfaces derived from natural amino acids

Paper ID Volume ID Publish Year Pages File Format Full-Text
8961 610 2009 5 PDF Available
Title
Ultra-low fouling peptide surfaces derived from natural amino acids
Abstract

This work demonstrated the ultra-low fouling natural peptides composed of certain negatively and positively charged residues such as glutamic acid (E) or aspartic acid (D) and lysine (K), in the form of either alternating or randomly mixed charge. These peptide-based materials are major candidates as biodegradable nonfouling materials since their final metabolized products are natural amino acids. Although hydrophilic materials can generally reduce nonspecific binding to a certain extent, it is very challenging to achieve ultra-low fouling, which is critical for many biomedical applications, such as medical implants, drug delivery carriers, and biosensors. Based on the design principle of uniformly mixed charges and the selection of appropriate amino acid residues, the natural peptides developed exhibit high resistance to nonspecific protein adsorption (<0.3 ng/cm2 adsorbed proteins) comparable to what is achieved by poly(ethylene glycol) (PEG)-based materials. Mixed charged groups, when uniformly distributed at the molecular level, can achieve ultra-low fouling properties similar to zwitterionic groups due to their strong hydration ability.

Keywords
Amino acids; Mixed charge; Peptides; Ultra-low fouling
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Ultra-low fouling peptide surfaces derived from natural amino acids
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biomaterials - Volume 30, Issue 29, October 2009, Pages 5892–5896
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us