News Column

New Oligopeptides Findings from University of Texas Outlined

June 20, 2014

By a News Reporter-Staff News Editor at Science Letter -- Fresh data on Peptides are presented in a new report. According to news reporting from Austin, Texas, by NewsRx journalists, research stated, "In our work toward developing ester-containing self-assembling peptides as soft biomaterials, we have found that a fluorenylmethoxycarbonyl (Fmoc)-conjugated alanine-lactic acid (Ala-Lac) sequence self-assembles into nanostructures that gel in water. This process occurs despite Fmoc-Ala-Lac's inability to interact with other Fmoc-Ala-Lac molecules via beta-sheet-like amide-amide hydrogen bonding, a condition previously thought to be crucial to the self-assembly of Fmoc-conjugated peptides."

The news correspondents obtained a quote from the research from the University of Texas, "Experimental comparisons of Fmoc-Ala-Lac to its self-assembling peptide sequence analogue Fmoc-Ala-Ala using a variety of microscopic, spectroscopic, and bulk characterization techniques demonstrate distinct features of the two systems and show that while angstrom-scale self-assembled structures are similar, their nanometer-scale size and morphological properties diverge and give rise to different bulk mechanical properties. Molecular dynamics simulations were performed to gain more insight into the differences between the two systems. An analysis of the hydrogen-bonding and solvent-surface interface properties of the simulated fibrils revealed that Fmoc-Ala-Lac fibrils are stronger and less hydrophilic than Fmoc-Ala-Ala fibrils. We propose that this difference in fibril amphiphilicity gives rise to differences in the higher-order assembly of fibrils into nanostructures seen in TEM. Importantly, we confirm experimentally that beta-sheet-type hydrogen bonding is not crucial to the self-assembly of short, conjugated peptides, and we demonstrate computationally that the amide bond in such systems may act mainly to mediate the solvation of the self-assembled single fibrils and therefore regulate a more extensive higher-order aggregation of fibrils."

According to the news reporters, the research concluded: "This work provides a basic understanding for future research in designing highly degradable self-assembling materials with peptide-like bioactivity for biomedical applications."

For more information on this research see: beta Sheets Not Required: Combined Experimental and Computational Studies of Self-Assembly and Gelation of the Ester-Containing Analogue of an Fmoc-Dipeptide Hydrogelator. Langmuir, 2014;30(18):5287-5296. Langmuir can be contacted at: Amer Chemical Soc, 1155 16TH St, NW, Washington, DC 20036, USA. (American Chemical Society -; Langmuir -

Our news journalists report that additional information may be obtained by contacting K.M. Eckes, Univ Texas Austin, Dept. of Biomed Engn, Austin, TX 78712, United States. Additional authors for this research include X.J. Mu, M.A. Ruehle, P.Y. Ren and L.J. Suggs (see also Peptides).

Keywords for this news article include: Texas, Gases, Austin, Elements, Hydrogen, Proteins, Dipeptides, Amino Acids, United States, Oligopeptides, Nanostructural, Nanostructures, Nanotechnology, Inorganic Chemicals, Emerging Technologies, North and Central America

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Source: Science Letter

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