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An interplay between electrostatic and polar interactions in peptide hydrogels
Author(s) -
Joyner Katherine,
Taraban Marc B.,
Feng Yue,
Yu Y. Bruce
Publication year - 2013
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22194
Subject(s) - chemistry , peptide , self healing hydrogels , polar , electrostatics , small angle x ray scattering , amino acid , electrostatic interaction , trifluoroacetic acid , biophysics , static electricity , chemical physics , chemical engineering , scattering , polymer chemistry , organic chemistry , biochemistry , astronomy , biology , optics , engineering , physics , electrical engineering
Inherent chemical programmability available in peptide‐based hydrogels has allowed diversity in the development of these materials for use in biomedical applications. Within the 20 natural amino acids, a range of chemical moieties are present. Here we used a mixing‐induced self‐assembly of two oppositely charged peptide modules to form a peptide‐based hydrogel. To investigate electrostatic and polar interactions in the hydrogel, we replace amino acids from the negatively charged acidic glutamic acid (E) to the uncharged polar glutamine (Q) on a negatively charged peptide module, while leaving the positively charged module unchanged. Using dynamic rheology, the mechanical properties of each hydrogel were investigated. It was found that the number, but not the location, of electrostatic interactions (E residues) dictate the elastic modulus ( G ′) of the hydrogel, compared to polar interactions (Q residues). Increased electrostatic interactions also promote faster peptide assembly into the hydrogel matrix, and result in the decrease of T 2 relaxation times of H 2 O and trifluoroacetic acid. Small‐angle X‐ray scattering (SAXS) showed that changing from electrostatic to polar interactions affects the ability to form fibrous networks: from the formation of elongated fibers to no fiber assembly. This study reveals the systematic effects that the incorporation of electrostatic and polar interactions have when programmed into peptide‐based hydrogel systems. These effects could be used to design peptide‐based biomaterials with predetermined properties. © 2012 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 100: 174–180, 2013.