Journal of Biomaterials Science, Polymer Edition ¶ 1998-01-01

Synthesis and characterization of polymer-(multi)-peptide conjugates for control of specific cell aggregation.

N Belcheva, S P Baldwin, W M Saltzman

文献索引：J. Biomater. Sci. Polym. Ed. 9(3) , 207-26, (1998)

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摘要

A new synthetic approach has been applied to obtain novel di-, tetra-, and (multi)-peptide containing polymer conjugates in quantitative yields with a high degree of conjugation. Bis-(N-hydroxysuccinimidyl) esters of PEG (Mw = 200, 600, 1400, 2000, and 3400) were synthesized and studied in a condensation reaction with synthetic peptides: glycine-glycine-tyrosine-arginine (GGYR), a model peptide, and glycine-arginine-glycine-aspartic acid-tyrosine (GRGDY), a sequence known to promote cell adhesion and aggregation. Tetra-substituted derivatives of PEG-based conjugates were synthesized by coupling L-aspartic acid and L-aspartyl-L-phenylalanine through a condensation procedure in organic media. Poly(acrylic acid) and co-polymers (Mw = 2000 and 5000) were studied as a model of multifunctional linear polymers in the reaction with L-tryptophan and GGYR. Alternative polymer-(multi)-peptide conjugates were successfully synthesized using Starburst dendrimer PAMAM (G = 3), 'short' and 'long'-chain PEG-based active esters and GRGDY. The structure of the intermediate precursors and peptide-conjugates was confirmed by spectral (UV-Vis, FTIR, H-NMR) and chromatographic (RP-HPLC and SEC) methods. By varying the properties of the interconnecting polymer--such as hydrophobicity, molecular weight, and functionality--a set of polymer-GRGDY conjugates was synthesized.