ÿþ<html> <head> <meta http-equiv="Content-Type" content="text/html; charset=windows-1251"> <meta name="Author" content> <meta name="Description" content="Contents and Abstracts of Journal Voprosy Meditsinskoi Khimii (Biomedical Chemistry)."> <meta name="KeyWords" content="polyamine metabolism, inhibitors of polyamine biosynthesis, ornitine decarboxylase,polyamine oxidase"> <meta name="GENERATOR" content="Microsoft FrontPage 6.0"> <title>Russian Journal: Biomeditsinskaya Khimiya (Biomedical Chemistry) Contents &amp; Abstracts</title> </head> <body background="../../4506/grayt.gif" bgcolor="#FFFFFF" text="#000000" link="#0000FF" vlink="#800080" alink="#0000FF"> <table border="0" cellpadding="0" cellspacing="0" width="100%"> <tr> <td valign="top"> <img alt="eng1.gif (176 bytes)" border="0" src="../pic/eng2.gif" width="39" height="16"><a href="../5201r/9r.htm"><img border="0" src="../pic/rus1.gif" width="39" height="16"></a></td> <td valign="top"><p align="center"><font size="5" face="Times New Roman CE"><b>Russian Journal</b></font></td> <td align="right" valign="top"><font face="Times New Roman CE">ISSN 0042-8809</font></td> </tr> </table> <div align="center"><center> <table border="0" cellpadding="0" cellspacing="0" width="100%"> <tr> <td valign="top"><font size="5" face="Times New Roman CE"><b>Biomeditsinskaya Khimiya</b></font></td> <td valign="top"><p align="right"><font size="5" face="Times New Roman CE"><b>Biomedical Chemistry</b></font><font face="Times New Roman CE"> </font></td> </tr> </table> </center></div> <hr> <p align="center"><font face="Times New Roman CE"> <a style="font-family: Arial; font-size: 10pt; font-weight: bold; color: #003399; text-decoration: none blink" href="../../default.htm">Home</a>&nbsp; </font><font face="Times New Roman">&#1472;&nbsp; <a style="font-family: Arial; font-size: 10pt; color: #003399; font-weight: bold; text-decoration: none" href="../../board.htm">Editorial Board</a> &#1472;&nbsp; <a style="text-decoration: none; color: #003399; font-family: Arial; font-size: 10pt; font-weight: bold" href="../../council.htm">International Advisory Board</a>&nbsp; &#1472;&nbsp; <a style="text-decoration: none; color: #003399; font-family: Arial; font-size: 10pt; font-weight: bold" href="../../aim.htm">Aim and Scope</a> &#1472;&nbsp;&nbsp; <a style="text-decoration: none; color: #003399; font-family: Arial; font-size: 10pt; font-weight: bold" href="../../content.htm">Contents and Abstracts</a>&nbsp; &#1472;&nbsp; <a style="text-decoration: none; color: #003399; font-family: Arial; font-size: 10pt; font-weight: bold" href="../../information.htm">Information for Authors</a> &#1472;&nbsp; <a style="text-decoration: none; color: #003399; font-family: Arial; font-size: 10pt; font-weight: bold" href="../../subscribe.htm">Subscribe Now</a></font></p> <hr> <p><b>Issue: <br> </b>Volume 52, issue 1</p> <p><strong> Title:</strong> BIODEGRADABLE MICROPARTICLES WITH IMMOBILIZED PEPTIDE FOR WOUND HEALING </p> <p class="MsoNormal"><strong> Authors: </strong> K.S. Stashevskaya<sup>1</sup>, E.A. Markvicheva<sup>1</sup>, S.M. Strukova<sup>2</sup>, A.V. Rusanova<sup>2</sup>, A.M. Makarova<sup>2</sup>, L.R. Gorbacheva<sup>2</sup>, I.A. Prudchenko<sup>1</sup>, V.P. Zubov<sup>1</sup>, K. Grandfis<sup>3</sup> </p> <p><b>Address: </b></p> <sup>1</sup>M.M. Shemyakin & Yu.A. Ovchinnikov Institute of Bioorganic Chemisty, Russian Academy of Sciences, Miklukho-Maklaya 16/10; Moscow, 117997 Russia; tel.: (495) 336-06-00; fax.: (495) 335-10-11; e-mail: <a href="mailto:kira_st@mail.ru">kira_st@mail.ru</a><br> <sup>2</sup>School of Biology, Moscow State University, Moscow, Russia<br> <sup>3</sup>Liege University, Belgium </p> <p><b>Abstract:</b> <br> Thrombin receptor agonist peptide (TRAP-6) may effectively replace thrombin for stimulation of damaged tissue regeneration. (Thrombin employment is limited by its high cost, instability and proinflammatory effect at high concentrations.) <br> Immobilization of TRAP-6 into a poly(D,L)-lactide-co-glycolide (PLGA)-based matrix can protect peptides from a destruction by peptidases located in a wound area, and can also provide controlled release of the peptide.<br> PLGA microparticles with immobilized peptide were produced by double emulsion/evaporation technique. <br> An observation of microparticle morphology by scanning electron microscopy highlighted that peptide immobilization resulted in the increase of the microparticle porosity. <br> TRAP-6 release kinetics was characterized by burst increase of TRAP-6 concentration in HEPES buffer solution (ðÍ 7.5) for first 2 hours from the beginning of the experiment, and TRAP-6 complete release occurred for 20 hours. <br> An investigation of TRAP-6 destruction by scanning electron microscopy revealed that the increase of microparticle size and surface porosity were observed already after 1 day of incubation in the buffer solution, and an aggregation of destructing microparticles was obvious by the 7th day of the incubation. Thus, peptide immobilization into PLGA microparticles can allow to develop a novel controlled release drug delivery system. <p><b>Key words:</b> immobilization, TRAP-6, PLGA microparticles, controlled release. </span></p> <b style="mso-bidi-font-weight:normal"> <hr> <p align="center"></b>[<a href="http://www.ibmc.msk.ru/pbmc/2006/5201/vol52is1.htm#9">Back</a>]<b style="mso-bidi-font-weight:normal"><b style="mso-bidi-font-weight:normal"></p> </b></b></font> </body> </html>