Peptoids for biomaterials science
Poly( N -substituted glycine) “peptoids” have conventionally been exploited for drug discovery and therapeutics due to their structural similarity to peptides, protease resistance, and relative ease of synthesis. This mini-review highlights recent reports of peptoid self-assembled nanostructures and...
Gespeichert in:
Veröffentlicht in: | Biomaterials science 2014-01, Vol.2 (5), p.627-633 |
---|---|
1. Verfasser: | |
Format: | Artikel |
Sprache: | eng |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 633 |
---|---|
container_issue | 5 |
container_start_page | 627 |
container_title | Biomaterials science |
container_volume | 2 |
creator | Lau, King Hang Aaron |
description | Poly(
N
-substituted glycine) “peptoids” have conventionally been exploited for drug discovery and therapeutics due to their structural similarity to peptides, protease resistance, and relative ease of synthesis. This mini-review highlights recent reports of peptoid self-assembled nanostructures and macromolecular interfaces relevant to biomaterials science. The results illustrate how the versatility of peptoid design and synthesis could be exploited to generate multifunctional, modular and precisely tunable biointerfaces and biomaterials. |
doi_str_mv | 10.1039/C3BM60269A |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2408844426</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2408844426</sourcerecordid><originalsourceid>FETCH-LOGICAL-c341t-ca93b464a4884051460be1adcafa03ddd6055b14325b88b5fb78c35b18523b273</originalsourceid><addsrcrecordid>eNpFUEtLxDAYDKLgsu7FX1BvIlS_JF_S9LgWX7CiBz2HJE0h0m5q0j3477eyi85lHgxzGEIuKdxS4PVdw-9fJTBZr0_IggFWJSqsT_80h3OyyvkLZlRVDZIuyNW7H6cY2lx0MRU2xMFMPgXT5yK74LfOX5CzbrZ-deQl-Xx8-Giey83b00uz3pSOI51KZ2puUaJBpRAERQnWU9M60xngbdtKEMJS5ExYpazobKUcnxMlGLes4ktyfdgdU_ze-TzpIWTn-95sfdxlzRDmZUQm5-rNoepSzDn5To8pDCb9aAr69wr9fwXfA3XyTnE</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2408844426</pqid></control><display><type>article</type><title>Peptoids for biomaterials science</title><source>Royal Society Of Chemistry Journals 2008-</source><source>Alma/SFX Local Collection</source><creator>Lau, King Hang Aaron</creator><creatorcontrib>Lau, King Hang Aaron</creatorcontrib><description>Poly(
N
-substituted glycine) “peptoids” have conventionally been exploited for drug discovery and therapeutics due to their structural similarity to peptides, protease resistance, and relative ease of synthesis. This mini-review highlights recent reports of peptoid self-assembled nanostructures and macromolecular interfaces relevant to biomaterials science. The results illustrate how the versatility of peptoid design and synthesis could be exploited to generate multifunctional, modular and precisely tunable biointerfaces and biomaterials.</description><identifier>ISSN: 2047-4830</identifier><identifier>EISSN: 2047-4849</identifier><identifier>DOI: 10.1039/C3BM60269A</identifier><language>eng</language><ispartof>Biomaterials science, 2014-01, Vol.2 (5), p.627-633</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c341t-ca93b464a4884051460be1adcafa03ddd6055b14325b88b5fb78c35b18523b273</citedby><cites>FETCH-LOGICAL-c341t-ca93b464a4884051460be1adcafa03ddd6055b14325b88b5fb78c35b18523b273</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids></links><search><creatorcontrib>Lau, King Hang Aaron</creatorcontrib><title>Peptoids for biomaterials science</title><title>Biomaterials science</title><description>Poly(
N
-substituted glycine) “peptoids” have conventionally been exploited for drug discovery and therapeutics due to their structural similarity to peptides, protease resistance, and relative ease of synthesis. This mini-review highlights recent reports of peptoid self-assembled nanostructures and macromolecular interfaces relevant to biomaterials science. The results illustrate how the versatility of peptoid design and synthesis could be exploited to generate multifunctional, modular and precisely tunable biointerfaces and biomaterials.</description><issn>2047-4830</issn><issn>2047-4849</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><recordid>eNpFUEtLxDAYDKLgsu7FX1BvIlS_JF_S9LgWX7CiBz2HJE0h0m5q0j3477eyi85lHgxzGEIuKdxS4PVdw-9fJTBZr0_IggFWJSqsT_80h3OyyvkLZlRVDZIuyNW7H6cY2lx0MRU2xMFMPgXT5yK74LfOX5CzbrZ-deQl-Xx8-Giey83b00uz3pSOI51KZ2puUaJBpRAERQnWU9M60xngbdtKEMJS5ExYpazobKUcnxMlGLes4ktyfdgdU_ze-TzpIWTn-95sfdxlzRDmZUQm5-rNoepSzDn5To8pDCb9aAr69wr9fwXfA3XyTnE</recordid><startdate>20140101</startdate><enddate>20140101</enddate><creator>Lau, King Hang Aaron</creator><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20140101</creationdate><title>Peptoids for biomaterials science</title><author>Lau, King Hang Aaron</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c341t-ca93b464a4884051460be1adcafa03ddd6055b14325b88b5fb78c35b18523b273</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lau, King Hang Aaron</creatorcontrib><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biomaterials science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lau, King Hang Aaron</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Peptoids for biomaterials science</atitle><jtitle>Biomaterials science</jtitle><date>2014-01-01</date><risdate>2014</risdate><volume>2</volume><issue>5</issue><spage>627</spage><epage>633</epage><pages>627-633</pages><issn>2047-4830</issn><eissn>2047-4849</eissn><abstract>Poly(
N
-substituted glycine) “peptoids” have conventionally been exploited for drug discovery and therapeutics due to their structural similarity to peptides, protease resistance, and relative ease of synthesis. This mini-review highlights recent reports of peptoid self-assembled nanostructures and macromolecular interfaces relevant to biomaterials science. The results illustrate how the versatility of peptoid design and synthesis could be exploited to generate multifunctional, modular and precisely tunable biointerfaces and biomaterials.</abstract><doi>10.1039/C3BM60269A</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 2047-4830 |
ispartof | Biomaterials science, 2014-01, Vol.2 (5), p.627-633 |
issn | 2047-4830 2047-4849 |
language | eng |
recordid | cdi_proquest_miscellaneous_2408844426 |
source | Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
title | Peptoids for biomaterials science |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-20T17%3A56%3A16IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Peptoids%20for%20biomaterials%20science&rft.jtitle=Biomaterials%20science&rft.au=Lau,%20King%20Hang%20Aaron&rft.date=2014-01-01&rft.volume=2&rft.issue=5&rft.spage=627&rft.epage=633&rft.pages=627-633&rft.issn=2047-4830&rft.eissn=2047-4849&rft_id=info:doi/10.1039/C3BM60269A&rft_dat=%3Cproquest_cross%3E2408844426%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2408844426&rft_id=info:pmid/&rfr_iscdi=true |