Loading…

Structure-Selectivity Relationships and Structure for a Peptide-Based Enantioselective Acylation Catalyst

Studies of analogues of a recently discovered enantioselective peptide-based catalyst for enantioselective acylation reactions have led to mechanistic insight and improved catalysts. Systematic replacement of each residue within the parent peptide with alanine of the appropriate stereochemistry allo...

Full description

Saved in:

Bibliographic Details
Published in:	Journal of the American Chemical Society 2004-06, Vol.126 (22), p.6967-6971
Main Authors:	Fierman, Matthew B, O'Leary, Daniel J, Steinmetz, Wayne E, Miller, Scott J
Format:	Article
Language:	English
Subjects:	Acylation Catalysis Chemical reactivity Chemistry Exact sciences and technology Kinetics Models, Molecular Molecular Structure Nuclear Magnetic Resonance, Biomolecular Organic chemistry Peptides - chemistry Peptides - metabolism Protein Conformation Reactivity and mechanisms Stereoisomerism Structure-Activity Relationship
Citations:	Items that this one cites Items that cite this one
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

cited_by	cdi_FETCH-LOGICAL-a445t-8c455adbf009211c261c6e57042a29cabcc473ffcb6fbaaa96e6f324d19f8553
cites	cdi_FETCH-LOGICAL-a445t-8c455adbf009211c261c6e57042a29cabcc473ffcb6fbaaa96e6f324d19f8553
container_end_page	6971
container_issue	22
container_start_page	6967
container_title	Journal of the American Chemical Society
container_volume	126
creator	Fierman, Matthew B O'Leary, Daniel J Steinmetz, Wayne E Miller, Scott J
description	Studies of analogues of a recently discovered enantioselective peptide-based catalyst for enantioselective acylation reactions have led to mechanistic insight and improved catalysts. Systematic replacement of each residue within the parent peptide with alanine of the appropriate stereochemistry allows for an unambiguous evaluation of the kinetic role of each amino acid side chain in the catalyst. The results of the alanine scan support a bifunctional catalysis mechanism at the heart of the origin of enantioselectivity. In addition, an experimentally derived solution structure of the peptide-based catalyst is presented that supports a key role for each residue within the peptide chain.
doi_str_mv	10.1021/ja049661c
format	article
fullrecord	<record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_71975483</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>71975483</sourcerecordid><originalsourceid>FETCH-LOGICAL-a445t-8c455adbf009211c261c6e57042a29cabcc473ffcb6fbaaa96e6f324d19f8553</originalsourceid><addsrcrecordid>eNpt0EFv0zAUB3ALMbEyOPAFkC8gcciwHdtJjlsZMDGJQis4Wi_Os3BJk2I7aP32GDXqOHCyLP_093t_Ql5wdsmZ4G-3wGSjNbePyIIrwQrFhX5MFowxUVS1Ls_J0xi3-SpFzZ-Qc654JWutF8SvU5hsmgIWa-zRJv_bpwP9ij0kPw7xh99HCkNHT466MVCgK9wn32FxDRE7ejPAkH2cI5Be2cMxgS4hQX-I6Rk5c9BHfD6fF2Tz_maz_Fjcff5wu7y6K0BKlYraSqWgax1jjeDciryWRlXl0UE0FlprZVU6Z1vtWgBoNGpXCtnxxtVKlRfk9TF2H8ZfE8Zkdj5a7HsYcJyiqXhTKVmXGb45QhvGGAM6sw9-B-FgODN_azWnWrN9OYdO7Q67Bzn3mMGrGUC00LsAg_XxH1eX-dcqu-LofEx4f3qH8NPoKhOzWa0Ne_d99eXTN23YQy7YaLbjFIZc3X8G_AOH_pzI</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>71975483</pqid></control><display><type>article</type><title>Structure-Selectivity Relationships and Structure for a Peptide-Based Enantioselective Acylation Catalyst</title><source>American Chemical Society:Jisc Collections:American Chemical Society Read & Publish Agreement 2022-2024 (Reading list)</source><creator>Fierman, Matthew B ; O'Leary, Daniel J ; Steinmetz, Wayne E ; Miller, Scott J</creator><creatorcontrib>Fierman, Matthew B ; O'Leary, Daniel J ; Steinmetz, Wayne E ; Miller, Scott J</creatorcontrib><description>Studies of analogues of a recently discovered enantioselective peptide-based catalyst for enantioselective acylation reactions have led to mechanistic insight and improved catalysts. Systematic replacement of each residue within the parent peptide with alanine of the appropriate stereochemistry allows for an unambiguous evaluation of the kinetic role of each amino acid side chain in the catalyst. The results of the alanine scan support a bifunctional catalysis mechanism at the heart of the origin of enantioselectivity. In addition, an experimentally derived solution structure of the peptide-based catalyst is presented that supports a key role for each residue within the peptide chain.</description><identifier>ISSN: 0002-7863</identifier><identifier>EISSN: 1520-5126</identifier><identifier>DOI: 10.1021/ja049661c</identifier><identifier>PMID: 15174866</identifier><identifier>CODEN: JACSAT</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Acylation ; Catalysis ; Chemical reactivity ; Chemistry ; Exact sciences and technology ; Kinetics ; Models, Molecular ; Molecular Structure ; Nuclear Magnetic Resonance, Biomolecular ; Organic chemistry ; Peptides - chemistry ; Peptides - metabolism ; Protein Conformation ; Reactivity and mechanisms ; Stereoisomerism ; Structure-Activity Relationship</subject><ispartof>Journal of the American Chemical Society, 2004-06, Vol.126 (22), p.6967-6971</ispartof><rights>Copyright © 2004 American Chemical Society</rights><rights>2004 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a445t-8c455adbf009211c261c6e57042a29cabcc473ffcb6fbaaa96e6f324d19f8553</citedby><cites>FETCH-LOGICAL-a445t-8c455adbf009211c261c6e57042a29cabcc473ffcb6fbaaa96e6f324d19f8553</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15837547$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15174866$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fierman, Matthew B</creatorcontrib><creatorcontrib>O'Leary, Daniel J</creatorcontrib><creatorcontrib>Steinmetz, Wayne E</creatorcontrib><creatorcontrib>Miller, Scott J</creatorcontrib><title>Structure-Selectivity Relationships and Structure for a Peptide-Based Enantioselective Acylation Catalyst</title><title>Journal of the American Chemical Society</title><addtitle>J. Am. Chem. Soc</addtitle><description>Studies of analogues of a recently discovered enantioselective peptide-based catalyst for enantioselective acylation reactions have led to mechanistic insight and improved catalysts. Systematic replacement of each residue within the parent peptide with alanine of the appropriate stereochemistry allows for an unambiguous evaluation of the kinetic role of each amino acid side chain in the catalyst. The results of the alanine scan support a bifunctional catalysis mechanism at the heart of the origin of enantioselectivity. In addition, an experimentally derived solution structure of the peptide-based catalyst is presented that supports a key role for each residue within the peptide chain.</description><subject>Acylation</subject><subject>Catalysis</subject><subject>Chemical reactivity</subject><subject>Chemistry</subject><subject>Exact sciences and technology</subject><subject>Kinetics</subject><subject>Models, Molecular</subject><subject>Molecular Structure</subject><subject>Nuclear Magnetic Resonance, Biomolecular</subject><subject>Organic chemistry</subject><subject>Peptides - chemistry</subject><subject>Peptides - metabolism</subject><subject>Protein Conformation</subject><subject>Reactivity and mechanisms</subject><subject>Stereoisomerism</subject><subject>Structure-Activity Relationship</subject><issn>0002-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><recordid>eNpt0EFv0zAUB3ALMbEyOPAFkC8gcciwHdtJjlsZMDGJQis4Wi_Os3BJk2I7aP32GDXqOHCyLP_093t_Ql5wdsmZ4G-3wGSjNbePyIIrwQrFhX5MFowxUVS1Ls_J0xi3-SpFzZ-Qc654JWutF8SvU5hsmgIWa-zRJv_bpwP9ij0kPw7xh99HCkNHT466MVCgK9wn32FxDRE7ejPAkH2cI5Be2cMxgS4hQX-I6Rk5c9BHfD6fF2Tz_maz_Fjcff5wu7y6K0BKlYraSqWgax1jjeDciryWRlXl0UE0FlprZVU6Z1vtWgBoNGpXCtnxxtVKlRfk9TF2H8ZfE8Zkdj5a7HsYcJyiqXhTKVmXGb45QhvGGAM6sw9-B-FgODN_azWnWrN9OYdO7Q67Bzn3mMGrGUC00LsAg_XxH1eX-dcqu-LofEx4f3qH8NPoKhOzWa0Ne_d99eXTN23YQy7YaLbjFIZc3X8G_AOH_pzI</recordid><startdate>20040609</startdate><enddate>20040609</enddate><creator>Fierman, Matthew B</creator><creator>O'Leary, Daniel J</creator><creator>Steinmetz, Wayne E</creator><creator>Miller, Scott J</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20040609</creationdate><title>Structure-Selectivity Relationships and Structure for a Peptide-Based Enantioselective Acylation Catalyst</title><author>Fierman, Matthew B ; O'Leary, Daniel J ; Steinmetz, Wayne E ; Miller, Scott J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a445t-8c455adbf009211c261c6e57042a29cabcc473ffcb6fbaaa96e6f324d19f8553</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Acylation</topic><topic>Catalysis</topic><topic>Chemical reactivity</topic><topic>Chemistry</topic><topic>Exact sciences and technology</topic><topic>Kinetics</topic><topic>Models, Molecular</topic><topic>Molecular Structure</topic><topic>Nuclear Magnetic Resonance, Biomolecular</topic><topic>Organic chemistry</topic><topic>Peptides - chemistry</topic><topic>Peptides - metabolism</topic><topic>Protein Conformation</topic><topic>Reactivity and mechanisms</topic><topic>Stereoisomerism</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fierman, Matthew B</creatorcontrib><creatorcontrib>O'Leary, Daniel J</creatorcontrib><creatorcontrib>Steinmetz, Wayne E</creatorcontrib><creatorcontrib>Miller, Scott J</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fierman, Matthew B</au><au>O'Leary, Daniel J</au><au>Steinmetz, Wayne E</au><au>Miller, Scott J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure-Selectivity Relationships and Structure for a Peptide-Based Enantioselective Acylation Catalyst</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2004-06-09</date><risdate>2004</risdate><volume>126</volume><issue>22</issue><spage>6967</spage><epage>6971</epage><pages>6967-6971</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><coden>JACSAT</coden><abstract>Studies of analogues of a recently discovered enantioselective peptide-based catalyst for enantioselective acylation reactions have led to mechanistic insight and improved catalysts. Systematic replacement of each residue within the parent peptide with alanine of the appropriate stereochemistry allows for an unambiguous evaluation of the kinetic role of each amino acid side chain in the catalyst. The results of the alanine scan support a bifunctional catalysis mechanism at the heart of the origin of enantioselectivity. In addition, an experimentally derived solution structure of the peptide-based catalyst is presented that supports a key role for each residue within the peptide chain.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>15174866</pmid><doi>10.1021/ja049661c</doi><tpages>5</tpages></addata></record>
fulltext	fulltext
identifier	ISSN: 0002-7863
ispartof	Journal of the American Chemical Society, 2004-06, Vol.126 (22), p.6967-6971
issn	0002-7863 1520-5126
language	eng
recordid	cdi_proquest_miscellaneous_71975483
source	American Chemical Society:Jisc Collections:American Chemical Society Read & Publish Agreement 2022-2024 (Reading list)
subjects	Acylation Catalysis Chemical reactivity Chemistry Exact sciences and technology Kinetics Models, Molecular Molecular Structure Nuclear Magnetic Resonance, Biomolecular Organic chemistry Peptides - chemistry Peptides - metabolism Protein Conformation Reactivity and mechanisms Stereoisomerism Structure-Activity Relationship
title	Structure-Selectivity Relationships and Structure for a Peptide-Based Enantioselective Acylation Catalyst
url	http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-13T01%3A45%3A22IST&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=Structure-Selectivity%20Relationships%20and%20Structure%20for%20a%20Peptide-Based%20Enantioselective%20Acylation%20Catalyst&rft.jtitle=Journal%20of%20the%20American%20Chemical%20Society&rft.au=Fierman,%20Matthew%20B&rft.date=2004-06-09&rft.volume=126&rft.issue=22&rft.spage=6967&rft.epage=6971&rft.pages=6967-6971&rft.issn=0002-7863&rft.eissn=1520-5126&rft.coden=JACSAT&rft_id=info:doi/10.1021/ja049661c&rft_dat=%3Cproquest_cross%3E71975483%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-a445t-8c455adbf009211c261c6e57042a29cabcc473ffcb6fbaaa96e6f324d19f8553%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=71975483&rft_id=info:pmid/15174866&rfr_iscdi=true