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Introducing D-amino acid or simple glycoside into small peptides to enable supramolecular hydrogelators to resist proteolysis.

ABSTRACT: Here we report the examination of two convenient strategies, the use of a d-amino acid residue or a glycoside segment, for increasing the proteolytic resistance of supramolecular hydrogelators based on small peptides. Our results show that the introduction of d-amino acid or glycoside to the peptides significantly increases the resistance of the hydrogelators against proteinase K, a powerful endopeptidase. The insertion of d-amino acid in the peptide backbone, however, results relatively low storage moduli of the hydrogels, likely due to the disruption of the superstructures of the molecular assembly. In contrast, the introduction of a glycoside to the C-terminal of peptide enhances the biostability of the hydrogelators without the significant decrease of the storage moduli of the hydrogels. This work suggests that the inclusion of a simple glycogen in hydrogelators is a useful approach to increase their biostability, and the gained understanding from the work may ultimately lead to development of hydrogels of functional peptides for biomedical applications that require long-term biostability.

SUBMITTER: Li X

PROVIDER: S-EPMC3472800 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature

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Introducing D-amino acid or simple glycoside into small peptides to enable supramolecular hydrogelators to resist proteolysis.

Li Xinming X Du Xuewen X Li Jiayang J Gao Yuan Y Pan Yue Y Shi Junfeng J Zhou Ning N Xu Bing B

Langmuir : the ACS journal of surfaces and colloids 20120904 37

Here we report the examination of two convenient strategies, the use of a d-amino acid residue or a glycoside segment, for increasing the proteolytic resistance of supramolecular hydrogelators based on small peptides. Our results show that the introduction of d-amino acid or glycoside to the peptides significantly increases the resistance of the hydrogelators against proteinase K, a powerful endopeptidase. The insertion of d-amino acid in the peptide backbone, however, results relatively low sto ...[more]

PMID: 22906360

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Project description:Supramolecular hydrogels formed by self-assembly of low molecular weight (LMW) compounds have been identified as promising materials for applications in tissue engineering and regenerative medicine. In many cases, the relationship between the chemical structure of the gelator and the emergent hydrogel properties is poorly understood. As a result, empirical screening strategies instead of rational design approaches are often relied upon to tune the emergent properties of the gels. Herein, we describe a novel strategy to identify improved phenylalanine (Phe) derived gelators using a focused empirical approach. Fluorenylmethoxycarbonyl (Fmoc) protected Phe derivatives are a privileged class of gelators that spontaneously self-assemble into fibrils that entangle to form a hydrogel network upon dissolution into water. However, the Fmoc group has been shown to have toxicity drawbacks for potential biological applications, requiring the identification of new N-terminal modifications that promote efficient self-assembly but lack the shortcomings of the Fmoc group. We previously discovered that fibrils in Fmoc-p-nitrophenylalanine (Fmoc-4-NO2-Phe) hydrogels transition to crystalline microtubes after several hours by a mechanism that involves the hierarchical assembly and fusion of the hydrogel fibrils. We hypothesized that this hierarchical crystallization behavior could form the basis of a screening approach to identify alternative N-terminal functional groups to replace Fmoc in Phe-derived LMW gelators. Specifically, screening N-terminal modifying groups for 4-NO2-Phe that stabilize the hydrogel state by preventing subsequent hierarchical crystallization would facilitate empirical identification of functional Fmoc replacements. To test this approach, we screened a small series of 4-NO2-Phe derivatives with various N-terminal modifying groups to determine if any provided stable LMW supramolecular hydrogels. All but one of the 4-NO2-Phe derivatives assembled into crystalline forms. Only the 1-naphthaleneacetic acid (1-Nap) 4-NO2-Phe derivative self-assembled into a stable hydrogel network. Additional Phe derivatives were modified by N-terminal 1-Nap groups to confirm the general potential of 1-Nap as a suitable replacement for Fmoc, and all derivatives formed stable hydrogels under similar conditions to their Fmoc-Phe counterparts. These results illustrate the potential of this approach to identify next-generation Phe-derived LMW gelators with improved emergent properties.

Dataset Information

Introducing D-amino acid or simple glycoside into small peptides to enable supramolecular hydrogelators to resist proteolysis.

Publications

Introducing D-amino acid or simple glycoside into small peptides to enable supramolecular hydrogelators to resist proteolysis.

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