<?xml version="1.0" encoding="UTF-8"?><?xml-stylesheet type="text/xsl" href="static/style.xsl"?><OAI-PMH xmlns="http://www.openarchives.org/OAI/2.0/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd"><responseDate>2026-09-18T20:09:02Z</responseDate><request verb="GetRecord" identifier="oai:dspace.mit.edu:1721.1/36746" metadataPrefix="dim">https://dspace.mit.edu/server/oai/request</request><GetRecord><record><header><identifier>oai:dspace.mit.edu:1721.1/36746</identifier><datestamp>2022-01-13T07:54:36Z</datestamp><setSpec>com_1721.1_7582</setSpec><setSpec>com_1721.1_7581</setSpec><setSpec>col_1721.1_131024</setSpec></header><metadata><dim:dim xmlns:dim="http://www.dspace.org/xmlns/dspace/dim" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:doc="http://www.lyncode.com/xoai" xsi:schemaLocation="http://www.dspace.org/xmlns/dspace/dim http://www.dspace.org/schema/dim.xsd">
   <dim:field mdschema="dc" element="contributor" qualifier="advisor" lang="en_US">Robert S. Langer.</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="author" lang="en_US">Hempel, Elizabeth (Elizabeth L.)</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="other" lang="en_US">Massachusetts Institute of Technology. Dept. of Mechanical Engineering.</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="department">Massachusetts Institute of Technology. Department of Mechanical Engineering</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="accessioned">2007-03-12T17:49:55Z</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="available">2007-03-12T17:49:55Z</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="copyright" lang="en_US">2006</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="issued" lang="en_US">2006</dim:field>
   <dim:field mdschema="dc" element="identifier" qualifier="uri">http://hdl.handle.net/1721.1/36746</dim:field>
   <dim:field mdschema="dc" element="identifier" qualifier="oclc" lang="en_US">78221940</dim:field>
   <dim:field mdschema="dc" element="description" lang="en_US">Thesis (S.B.)--Massachusetts Institute of Technology, Dept. of Mechanical Engineering, 2006.</dim:field>
   <dim:field mdschema="dc" element="description" lang="en_US">Includes bibliographical references (p. 18).</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="abstract" lang="en_US">Biologically active materials providing a range of applications from tissue engineering to microdevices have begun to revolutionize biomedical science. New chemistries, however, must be developed for functionalization of these materials with each different molecule. This paper explores a technique for developing multi-functional, biologically active hydrogels utilizing the high streptavidin-biotin binding affinity. Streptavidin was conjugated to acryl-PEG-N-hydroxysuccinimide, a commercially available molecule that allows chemical binding to poly(ethylene glycol) (PEG) diacrylate and dextran acrylate hydrogels. Such gels were made by photocrosslinking solutions of APN and streptavidin conjugated at various molar ratios, along with a gelling polymer under an ultraviolet (UV) lamp. Acryl group conjugation was confirmed through high performance liquid chromatography (HPLC) and mass spectrometry. Protein binding was assayed through the use of rhodamine-labeled streptavidin and fluorescent microscopy. Gels were incubated overnight in solution to determine diffusion. After 7 days, PEG showed no diffusion while dextran acrylate demonstrated 100% protein loss.</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="statementofresponsibility" lang="en_US">by Elizabeth Hempel.</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="degree" lang="en_US">S.B.</dim:field>
   <dim:field mdschema="dc" element="format" qualifier="extent" lang="en_US">18 p.</dim:field>
   <dim:field mdschema="dc" element="language" qualifier="iso" lang="en_US">eng</dim:field>
   <dim:field mdschema="dc" element="publisher" lang="en_US">Massachusetts Institute of Technology</dim:field>
   <dim:field mdschema="dc" element="rights" lang="en_US">M.I.T. theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission.</dim:field>
   <dim:field mdschema="dc" element="rights" qualifier="uri">http://dspace.mit.edu/handle/1721.1/7582</dim:field>
   <dim:field mdschema="dc" element="subject" lang="en_US">Mechanical Engineering.</dim:field>
   <dim:field mdschema="dc" element="title" lang="en_US">A potential route to hydrogel multifunctionalization utilizing encapsulation of acrylate-conjugated streptavidin</dim:field>
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   	&lt;Title>A potential route to hydrogel multifunctionalization utilizing encapsulation of acrylate-conjugated streptavidin&lt;/Title>
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   	&lt;PublicationDate>2006&lt;/PublicationDate>
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        	&lt;DisplayName>Hempel, Elizabeth (Elizabeth L.)&lt;/DisplayName>
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    &lt;Keyword>Mechanical Engineering.&lt;/Keyword>
   	&lt;Abstract>Biologically active materials providing a range of applications from tissue engineering to microdevices have begun to revolutionize biomedical science. New chemistries, however, must be developed for functionalization of these materials with each different molecule. This paper explores a technique for developing multi-functional, biologically active hydrogels utilizing the high streptavidin-biotin binding affinity. Streptavidin was conjugated to acryl-PEG-N-hydroxysuccinimide, a commercially available molecule that allows chemical binding to poly(ethylene glycol) (PEG) diacrylate and dextran acrylate hydrogels. Such gels were made by photocrosslinking solutions of APN and streptavidin conjugated at various molar ratios, along with a gelling polymer under an ultraviolet (UV) lamp. Acryl group conjugation was confirmed through high performance liquid chromatography (HPLC) and mass spectrometry. Protein binding was assayed through the use of rhodamine-labeled streptavidin and fluorescent microscopy. Gels were incubated overnight in solution to determine diffusion. After 7 days, PEG showed no diffusion while dextran acrylate demonstrated 100% protein loss.&lt;/Abstract>
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