<?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>2026-09-20T01:35:23Z</responseDate><request verb="GetRecord" identifier="oai:dspace.mit.edu:1721.1/121606" metadataPrefix="dim">https://dspace.mit.edu/server/oai/request</request><GetRecord><record><header><identifier>oai:dspace.mit.edu:1721.1/121606</identifier><datestamp>2026-06-16T18:51:43Z</datestamp><setSpec>com_1721.1_7582</setSpec><setSpec>com_1721.1_7581</setSpec><setSpec>col_1721.1_131022</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">Alfredo Alexander-Katz.</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="author" lang="en_US">Tahir, Mukarram Ahmad.</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="other" lang="en_US">Massachusetts Institute of Technology. Department of Materials Science and Engineering.</dim:field>
   <dim:field mdschema="dc" element="contributor" qualifier="department" lang="en_US">Massachusetts Institute of Technology. Department of Materials Science and Engineering</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="accessioned">2019-07-12T17:41:15Z</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="available">2019-07-12T17:41:15Z</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="copyright" lang="en_US">2019</dim:field>
   <dim:field mdschema="dc" element="date" qualifier="issued" lang="en_US">2019</dim:field>
   <dim:field mdschema="dc" element="identifier" qualifier="uri">https://hdl.handle.net/1721.1/121606</dim:field>
   <dim:field mdschema="dc" element="identifier" qualifier="oclc" lang="en_US">1102047979</dim:field>
   <dim:field mdschema="dc" element="description" lang="en_US">Thesis: Ph. D., Massachusetts Institute of Technology, Department of Materials Science and Engineering, 2019</dim:field>
   <dim:field mdschema="dc" element="description" lang="en_US">Cataloged from PDF version of thesis.</dim:field>
   <dim:field mdschema="dc" element="description" lang="en_US">Includes bibliographical references (pages [121]-140).</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="abstract" lang="en_US">Gold nanoparticles with amphiphilic surface functionalization have been shown to spontaneously fuse with lipid bilayers through a non-endocytic mechanism that generates minimal membrane perturbation. The membrane translocation capability of these nanoparticles makes them attractive candidates for engineering clinical applications that operate on a single-cell resolution. In particular, the physiochemical similarity between these nanoparticles and membrane-bound and free-circulating proteins suggests a possibility for designing nanostructures that can function as synthetic alternatives to proteins. In this thesis, we demonstrate how molecular simulation techniques have allowed us to tackle this engineering challenge and develop nanoparticles that can modulate fusion between lipid membranes, transport hydrophobic small molecules to lipid-bound compartments, and modify the permeability of lipid membranes. These are concrete realizations of nanoparticles functioning as protein mimics, and unlock new avenues of research on how nanomaterials can be designed from first principles to perform targeted functions in biological systems.</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="statementofresponsibility" lang="en_US">by Mukarram Ahmad Tahir.</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="degree" lang="en_US">Ph.D.</dim:field>
   <dim:field mdschema="dc" element="description" qualifier="collection" lang="en_US">Ph.D. Massachusetts Institute of Technology, Department of Materials Science and Engineering</dim:field>
   <dim:field mdschema="dc" element="format" qualifier="extent" lang="en_US">140 pages</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">MIT theses are protected by copyright. They may be viewed, downloaded, or printed from this source but further reproduction or distribution in any format is prohibited without written permission.</dim:field>
   <dim:field mdschema="dc" element="rights" qualifier="uri" lang="en_US">http://dspace.mit.edu/handle/1721.1/7582</dim:field>
   <dim:field mdschema="dc" element="subject" lang="en_US">Materials Science and Engineering.</dim:field>
   <dim:field mdschema="dc" element="title" lang="en_US">Protein mimetic nanoparticles</dim:field>
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   <dim:field mdschema="mit" element="thesis" qualifier="degree" lang="en_US">Doctoral</dim:field>
   <dim:field mdschema="mit" element="thesis" qualifier="department" lang="en_US">MatSci</dim:field>
   <dim:field mdschema="others" element="access-status">unknown</dim:field>
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   	&lt;Title>Protein mimetic nanoparticles&lt;/Title>
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   	&lt;PublicationDate>2019&lt;/PublicationDate>
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        	&lt;DisplayName>Tahir, Mukarram Ahmad.&lt;/DisplayName>
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            &lt;DisplayName>Massachusetts Institute of Technology&lt;/DisplayName>
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    &lt;License>http://dspace.mit.edu/handle/1721.1/7582&lt;/License>
    &lt;Keyword>Materials Science and Engineering.&lt;/Keyword>
   	&lt;Abstract>Gold nanoparticles with amphiphilic surface functionalization have been shown to spontaneously fuse with lipid bilayers through a non-endocytic mechanism that generates minimal membrane perturbation. The membrane translocation capability of these nanoparticles makes them attractive candidates for engineering clinical applications that operate on a single-cell resolution. In particular, the physiochemical similarity between these nanoparticles and membrane-bound and free-circulating proteins suggests a possibility for designing nanostructures that can function as synthetic alternatives to proteins. In this thesis, we demonstrate how molecular simulation techniques have allowed us to tackle this engineering challenge and develop nanoparticles that can modulate fusion between lipid membranes, transport hydrophobic small molecules to lipid-bound compartments, and modify the permeability of lipid membranes. These are concrete realizations of nanoparticles functioning as protein mimics, and unlock new avenues of research on how nanomaterials can be designed from first principles to perform targeted functions in biological systems.&lt;/Abstract>
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