Amino acids and peptides. LXIV. Infrared spectra of substituted 2,5-piperazinediones and the detection of cis-peptide bonds in diastereomeric cyclohexapeptides

Bláha, K.; Smolíková, J.; Vítek, A.

doi:10.1135/cccc19664296

Cited by 30 publications

(9 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Model building studies with space-filling atomic models suggested that cyclocystine has a cis-amide group, and if this is so it could imply some instability of this bond to acid hydrolysis. An infrared spectrum of our sample of cyclocystine showed bands at 1470cm.-1 and 1295cm.-', which are characteristic of cis-amide bonds (Blaha, Smolikova & Vitek, 1966) and thus reinforced this possibility.…”

supporting

confidence: 64%

Disulphide interchange reactions involving cyclocystine and their relevance to problems of α-keratin structure

Lindley

Haylett

1968

Biochemical Journal

View full text Add to dashboard Cite

supporting

confidence: 64%

Disulphide interchange reactions involving cyclocystine and their relevance to problems of α-keratin structure

Lindley

Haylett

1968

Biochemical Journal

View full text Add to dashboard Cite

“…bond (14), and is suitable for detecting a cis peptide bond among trans peptide bonds (15), appears at 1355 cm-' in poly(L-proline) I (16), from 1325 to 1343 cm-' in diketopiperazines (15), and at 1340 cm-' in N-methyl acetamide (14); on the other hand, the trans amide III band appears around 1250 cm-' (15). As can be seen in Fig.…”

Section: Methodsmentioning

confidence: 84%

Nuclear Magnetic Resonance Studies of Lysine-Vasopressin: Structural Constraints

Dreele¹,

Brewster²,

Bovey³

et al. 1971

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

The 220-MHz proton NMR spectra of lysine-vasopressin and some related compounds are examined in deuterated dimethyl sulfoxide to obtain structural information that must be satisfied by any proposed conformation of the molecule. This structural information is in the form of dihedral angles (for rotation about the NH-CaH bonds) from coupling constants, possible hydrogen bonding of the CONH2 and backbone amide groups from the temperature-dependence of the chemical shift, and aromatic ring-aromatic ring interaction from the effect of the magnetically anisotropic groups on the chemical shift.

show abstract

“…Differences were not observed in absorption regions associated with cis peptide bonds. 13 Similarity of absorption at 1450 cm-' (region of the cis amide I1 band) is particularly significant because effects are not obscured by absorption associated with methylene deformation which also occurs in the 1450 cm-l range. Nuclear magnetic resonance (NMR) spectroscopy has been used to distinguish between peptide diastereoisomers, with upfield shifts observed in L,D isomers relative to the L,L form in NMR spectra of dipeptides containing one or more aromatic residues.…”

Section: Resultsmentioning

confidence: 99%

Conformation of dipeptides

Lande

1969

Biopolymers

View full text Add to dashboard Cite

spopsisThe amide bond in L,L-and L,m-chloropropionylalanine methyl ester is shown to be trans by molar polarization and infrared spectroscopy. In these dipeptide diastereoisomer analogues, therefore, differences in physical properties, i.e., melting points, crystalline forms, gas chromatographic mobilities, etc., depend on preferred molecular conformations and not peptide bond configuration. Nuclear magnetic resonance spectra of both compounds were identical, indicating that no major chemical environment differences exist which might have resulted from dissimilar side group interactions. Based on the data reported here and those of others, most dipeptide conformations can be eliminated because of contradiction with limits set by experimental or theoretical considerations. Of the remaining conformational possibilities, a single pair accounts for observed physical differences in dipeptide diastereoisomers, free or blocked. The preferred form contains a-hydrogens trans to each other and in the plane of the peptide bond. In this conformation, RLR* and amino-carboxyl distances are minimal in L,D dillstereomers and maximal in L,L forms.

show abstract

Amino acids and peptides. LXIV. Infrared spectra of substituted 2,5-piperazinediones and the detection of cis-peptide bonds in diastereomeric cyclohexapeptides

Cited by 30 publications

References 0 publications

Disulphide interchange reactions involving cyclocystine and their relevance to problems of α-keratin structure

Disulphide interchange reactions involving cyclocystine and their relevance to problems of α-keratin structure

Nuclear Magnetic Resonance Studies of Lysine-Vasopressin: Structural Constraints

Conformation of dipeptides

Contact Info

Product

Resources

About