Study Data from University of California Update Knowledge of Peptides and Proteins (Multimeric Disintegrin Protein Polymer Fusions That Target Tumor Vasculature)
By a News Reporter-Staff News Editor at Science Letter -- Research findings on Peptides are discussed in a new report. According to news originating from Los Angeles, California, by NewsRx correspondents, research stated, "Recombinant protein therapeutics have increased in number and frequency since the introduction of human insulin, 25 years ago. Presently, proteins and peptides are commonly used in the clinic."
Our news journalists obtained a quote from the research from the University of California, "However, the incorporation of peptides into clinically approved nanomedicines has been limited. Reasons for this include the challenges of decorating pharmaceutical-grade nanoparticles with proteins by a process that is robust, scalable, and cost-effective. As an alternative to covalent bioconjugation between a protein and nanoparticle, we report that biologically active proteins may themselves mediate the formation of small multimers through steric stabilization by large protein polymers. Unlike multistep purification and bioconjugation, this approach is completed during biosynthesis. As proof-of-principle, the disintegrin protein called vicrostatin (VCN) was fused to an elastin-like polypeptide (A192). A significant fraction of fusion proteins self-assembled into multimers with a hydrodynamic radius of 15.9 nm. The A192-VCN fusion proteins compete specifically for cell-surface integrins on human umbilical vein endothelial cells (HUVECs) and two breast cancer cell lines, MDA-MB-231 and MDA-MB-435. Confocal microscopy revealed that, unlike linear RGD-containing protein polymers, the disintegrin fusion protein undergoes rapid cellular internalization. To explore their potential clinical applications, fusion proteins were characterized using small animal positron emission tomography (microPET). Passive tumor accumulation was observed for control protein polymers; however, the tumor accumulation of A192-VCN was saturable, which is consistent with integrin-mediated binding. The fusion of a protein polymer and disintegrin results in a higher intratumoral contrast compared to free VCN or A192 alone."
According to the news editors, the research concluded: "Given the diversity of disintegrin proteins with specificity for various cell-surface integrins, disintegrin fusions are a new source of biomaterials with potential diagnostic and therapeutic applications."
For more information on this research see: Multimeric Disintegrin Protein Polymer Fusions That Target Tumor Vasculature. Biomacromolecules, 2014;15(7):2347-2358. 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 S.M. Janib, University of California, Viterbi Sch Engn, Dept. of Biomed Engn, Los Angeles, CA 90089, United States. Additional authors for this research include J.A. Gustafson, R.O. Minea, S.D. Swenson, S.L. Liu, M.K. Pastuszka, L.L. Lock, H.G. Cui, F.S. Markland, P.S. Conti, Z.B. Li and J.A. MacKay (see also Peptides).
Keywords for this news article include: Peptides, Proteins, California, Los Angeles, Amino Acids, Disintegrins, United States, North and Central America
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