By a News Reporter-Staff News Editor at Science Letter -- Research findings on Proteins are discussed in a new report. According to news originating from Baltimore, Maryland, by NewsRx correspondents, research stated, "One-dimensional nanostructures formed by self-assembly of small molecule peptides have been extensively explored for use as biomaterials in various biomedical contexts. However, unlike individual peptides that can be designed to be specifically degradable by enzymes/proteases of interest, their self-assembled nanostructures, particularly those rich in beta-sheets, are generally resistant to enzymatic degradation because the specific cleavage sites are often embedded inside the nanostructures."
Our news journalists obtained a quote from the research from Johns Hopkins University, "We report here on the rational design of beta-sheet rich supramolecular filaments that can specifically dissociate into less stable micellar assemblies and monomers upon treatment with matrix metalloproteases-2 (MMP-2). Through linkage of an oligoproline segment to an amyloid-derived peptide sequence, we first synthesized an amphiphilic peptide that can undergo a rapid morphological transition in response to pH variations. We then used MMP-2 specific peptide substrates as multivalent cross-linkers to covalently fix the amyloid-like filaments in the self-assembled state at pH 4.5. Our results show that the cross-linked filaments are stable at pH 7.5 but gradually break down into much shorter filaments upon cleavage of the peptidic cross-linkers by MMP-2."
According to the news editors, the research concluded: "We believe that the reported work presents a new design platform for the creation of amyloid-like supramolecular filaments responsive to enzymatic degradation."
For more information on this research see: Rational Design of MMP Degradable Peptide-Based Supramolecular Filaments. Biomacromolecules, 2014;15(4):1419-1427. Biomacromolecules can be contacted at: Amer Chemical Soc, 1155 16TH St, NW, Washington, DC 20036, USA. (American Chemical Society - www.acs.org; Biomacromolecules - www.pubs.acs.org/journal/bomaf6)
The news correspondents report that additional information may be obtained from Y.A. Lin, Johns Hopkins University, Inst NanoBiotechnol, Baltimore, MD 21218, United States. Additional authors for this research include Y.C. Ou, A.G. Cheetham and H.G. Cui (see also Proteins).
Keywords for this news article include: Amyloid, Maryland, Proteins, Baltimore, United States, Nanostructural, Nanostructures, Nanotechnology, Supramolecular, Emerging Technologies, North and Central America
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