Site-specific N-terminus conjugation of poly(mPEG1100) methacrylates to salmon calcitonin: synthesis and preliminary biological evaluation

Autor:	Oksana I. Leszczyszyn, Rajan K. Randev, Claudia A. Blindauer, David M. Haddleton, Odin Keiper, David J. Brayden, Sinéad M. Ryan, Claire T. Sayers, Giuseppe Mantovani
Rok vydání:	2009
Předmět:	chemistry.chemical_classification Biological activity Peptide General Chemistry Polyethylene glycol Conjugated system Condensed Matter Physics Reductive amination In vitro chemistry.chemical_compound chemistry Biochemistry Polymerization Macromolecule
Zdroj:	Soft Matter. 5:3038
ISSN:	1744-6848 1744-683X
DOI:	10.1039/b905335b
Popis:	Recent advances in polymerization strategies have led to the development of novel polymer–(poly)peptide biohybrid materials with potential application in the field of macromolecular therapeutics. In this current work, comb-shaped α-aldehyde poly(monomethoxy polyethylene glycol)methacrylates (p(mPEG)MA) with molecular masses in the 6.5–109 kDa range were prepared and conjugated, via reductive amination, to the Cys1N-terminus of salmon calcitonin (sCT), a calcitropic hormone currently administered for the treatment of a number of hypercalcaemia-related diseases. The conjugation site was determined by tryptic digestion of the sCT–p(mPEG1100)MA biohybrids in conjunction with LC-MS MALDI-TOF spectrometry. Preliminary in vitro biological tests show that the polymer conjugation does not interfere with the biological activity of the sCT.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::2a8c07f881baf6f51ba887674ebee6ec https://doi.org/10.1039/b905335b Zobrazit plný text záznamu