Synthesis and peptide bond orientation in tetrapeptides containing L -azetidine-2-carboxylic acid and L -proline
dc.contributor.author | Tsai, F. -H. | en_US |
dc.contributor.author | Overberger, Charles Gilbert | en_US |
dc.contributor.author | Zand, Robert | en_US |
dc.date.accessioned | 2006-04-28T16:28:03Z | |
dc.date.available | 2006-04-28T16:28:03Z | |
dc.date.issued | 1990 | en_US |
dc.identifier.citation | Tsai, F.-H.; Overberger, C. G.; Zand, R. (1990)."Synthesis and peptide bond orientation in tetrapeptides containing L -azetidine-2-carboxylic acid and L -proline." Biopolymers 30(11-12): 1039-1049. <http://hdl.handle.net/2027.42/37858> | en_US |
dc.identifier.issn | 0006-3525 | en_US |
dc.identifier.issn | 1097-0282 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/37858 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2081265&dopt=citation | en_US |
dc.description.abstract | The role of the amino acid proline in influencing the secondary and tertiary structure of proteins and polypeptides has been an area of active study for many years. We have investigated this problem by incorporating the four-membered ring amino acid, azetidine-2-carboxylic acid, into some proline polypeptides. An adjunct to the synthesis of the peptides was the synthesis of azetidine-2-carboxylic acid and its resolution. We developed an improved synthesis of N-benzhydryl-2-carbobenzyloxy azetidine, an essential intermediate required for the synthesis of L azetidine-2-carboxylic acid. This amino acid was subsequently obtained via the partial hydrogenation of the N-benzhydryl compound, under mild conditions. Our ability to isolate the intermediate N-benzhydryl-2-carboxylic acid demonstrated that the rate of cleavage of the O -benzyl ester group in this molecule is faster than the cleavage of the N-benzhydryl group. The tetrapeptides, Boc-( L Pro) 3 - L Aze-Opcp, and Boc-( L Aze- L Pro)2-Opcp (Boc: t -butoxycarbonyl; Pro: praline; Aze: azetidine-2-carboxyl acid; Opcp: pentachlorophenyl), were prepared using traditional solution peptide synthesis. They were characterized by direct chemical ionization-mass spectrometry, CD spectra, and 13 C- and 1 H-nmr spectroscopy. The assessment of the secondary structure assessment of the two peptides using the methods noted above has led us to conclude that the compound Boc-( L -Aze- L Pro) 2 -Opcp, in trifluoroethanol, has an all- cis peptide bond conformation with φ and Ψ torsion angles compatible with a left-handed helix. The secondary structure assessment of the peptide Boc-( L Pro) 3 - L Aze-Opcp, in chloroform or trifluoroethanol, leads to an assignment of both cis and trans peptide bonds as being present in the peptide. We have interpreted this latter finding as indicating that the introduction of the azetidine group into a peptide containing three consecutive praline residues in a linear sequence perturbs the normal proline peptide secondary structure in this tetrapeptide. | en_US |
dc.format.extent | 884868 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Wiley Subscription Services, Inc., A Wiley Company | en_US |
dc.subject.other | Chemistry | en_US |
dc.subject.other | Polymer and Materials Science | en_US |
dc.title | Synthesis and peptide bond orientation in tetrapeptides containing L -azetidine-2-carboxylic acid and L -proline | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Macromolecular Research Center and Biophysics Research Division, Institute of Science and Technology, Department of Biological Chemistry and Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109-2099 | en_US |
dc.contributor.affiliationum | Macromolecular Research Center and Biophysics Research Division, Institute of Science and Technology, Department of Biological Chemistry and Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109-2099 | en_US |
dc.contributor.affiliationum | Macromolecular Research Center and Biophysics Research Division, Institute of Science and Technology, Department of Biological Chemistry and Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109-2099 ; Macromolecular Research Center and Biophysics Research Division, Institute of Science and Technology, Department of Biological Chemistry and Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109-2099 | en_US |
dc.identifier.pmid | 2081265 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/37858/1/360301105_ftp.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1002/bip.360301105 | en_US |
dc.identifier.source | Biopolymers | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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