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Synthetic Polypeptides (synthetic + polypeptide)

Distribution by Scientific Domains

Chemistry	80%

Selected Abstracts

Dual Stimuli-Responsive Supramolecular Polypeptide-Based Hydrogel and Reverse Micellar Hydrogel Mediated by Host,Guest Chemistry

ADVANCED FUNCTIONAL MATERIALS, Issue 4 2010
Yi Chen
Abstract Versatile strategies are currently being discovered for the fabrication of synthetic polypeptide-based hybrid hydrogels, which have potential applications in polymer therapeutics and regenerative medicine. Herein, a new concept,the reverse micellar hydrogel,is introduced, and a versatile strategy is provided for fabricating supramolecular polypeptide-based normal micellar hydrogel and reverse micellar hydrogels from the same polypeptide-based copolymer via the cooperation of host,guest chemistry and hydrogen-bonding interactions. The supramolecular hydrogels are thoroughly characterized, and a mechanism for their self-assembly is proposed. These hydrogels can respond to dual stimuli,temperature and pH,and their mechanical and controlled drug-release properties can be tuned by the copolymer topology and the polypeptide composition. The reverse micellar hydrogel can load 10% of the anticancer drug doxorubicin hydrochloride (DOX) and sustain DOX release for 45 days, indicating that it could be useful as an injectable drug delivery system. [source]

Toward the semisynthesis of multidomain transmembrane receptors: Modification of Eph tyrosine kinases

PROTEIN SCIENCE, Issue 10 2008
Nikhil Singla
Abstract Expressed protein ligation (EPL) is a protein engineering approach that allows the modification or assembly of a target protein from multiple recombinant and synthetic polypeptides. EPL has been previously used to modify intracellular proteins and small integral membrane proteins for structural and functional studies. Here we describe the semisynthetic site-specific modification of the complete, multidomain extracellular regions of both A and B classes of Eph receptor tyrosine kinases. We show that the ectodomains of these receptors can be ligated to different peptides under carefully established experimental conditions, while their biological activity is retained. This work extends the boundaries of the EPL technique for semisynthesis of multidomain, extracellular, disulfide-bonded, and glycosylated proteins and highlights its potential application for reconstituting entire single-pass transmembrane proteins. [source]

Sequence- and site-specific photodissociation at 266,nm of protonated synthetic polypeptides containing a tryptophanyl residue

RAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 22 2004
Joo Yeon Oh
Photodissociation at 266,nm of protonated synthetic polypeptides containing a tryptophanyl residue was investigated using a homebuilt tandem time-of-flight mass spectrometer equipped with a matrix-assisted laser desorption/ionization source. Efficient photodissociation of the protonated peptides was demonstrated. Most of the intense peaks in the laser-induced tandem mass spectra were sequence ions. Furthermore, sequence ions due to cleavages at all the peptide bonds were observed; this is a feature of the technique that is particularly useful for peptide sequencing. Fragmentations at both ends of the tryptophanyl residue were especially prevalent, which can be useful for location of the tryptophanyl chromophore in a peptide. Copyright © 2004 John Wiley & Sons, Ltd. [source]

Structural characterization of the N-terminal mineral modification domains from the molluscan crystal-modulating biomineralization proteins, AP7 and AP24

BIOPOLYMERS, Issue 5 2004
Brandon A. Wustman
Abstract The AP7 and AP24 proteins represent a class of mineral-interaction polypeptides that are found in the aragonite-containing nacre layer of mollusk shell (H. rufescens). These proteins have been shown to preferentially interfere with calcium carbonate mineral growth in vitro. It is believed that both proteins play an important role in aragonite polymorph selection in the mollusk shell. Previously, we demonstrated the 1,30 amino acid (AA) N-terminal sequences of AP7 and AP24 represent mineral interaction/modification domains in both proteins, as evidenced by their ability to frustrate calcium carbonate crystal growth at step edge regions. In this present report, using free N-terminal, C, -amide "capped" synthetic polypeptides representing the 1,30 AA regions of AP7 (AP7-1 polypeptide) and AP24 (AP24-1 polypeptide) and NMR spectroscopy, we confirm that both N-terminal sequences possess putative Ca (II) interaction polyanionic sequence regions (2 × ,DD, in AP7-1, ,DDDED, in AP24-1) that are random coil-like in structure. However, with regard to the remaining sequences regions, each polypeptide features unique structural differences. AP7-1 possesses an extended ,-strand or polyproline type II-like structure within the A11,M10, S12,V13, and S28,I27 sequence regions, with the remaining sequence regions adopting a random-coil-like structure, a trait common to other polyelectrolyte mineral-associated polypeptide sequences. Conversely, AP24-1 possesses random coil-like structure within A1,S9 and Q14,N16 sequence regions, and evidence for turn-like, bend, or loop conformation within the G10,N13, Q17,N24, and M29,F30 sequence regions, similar to the structures identified within the putative elastomeric proteins Lustrin A and sea urchin spicule matrix proteins. The similarities and differences in AP7 and AP24 N-terminal domain structure are discussed with regard to joint AP7,AP24 protein modification of calcium carbonate growth. © 2004 Wiley Periodicals, Inc. Biopolymers 2004 [source]