Über Peptidsynthesen, 31. Chromatographische Trennung einiger diastereomerer Dipeptide und Betrachtungen zur Konformation

Wieland, Theodor; Bende, H.

doi:10.1002/cber.19650980222

Cited by 60 publications

(9 citation statements)

References 19 publications

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“…In the case of dipeptides these results find an aromatic function (20)(21)(22). It is known from a ready explanation if the conformation of both the work of Kenner and co-workers (23)(24)(25) that L,L-and L,D-peptides is assumed t o be of the peptides containing some D-amino acids show a P-type, 4a and b (19 …”

Section: Resultsmentioning

confidence: 93%

Peptide Conformations. I. Nuclear Magnetic Resonance Study of the Carbamate Reaction of Amino Acids and Peptides

Lemieux¹,

Barton²

1971

Can. J. Chem.

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Nuclear magnetic resonance spectroscopy has been applied to the study of carbamate formation in solutions of amino acids and peptides in a carbonate-bicarbonate system. The possible conformations of these carbamates are discussed in terms of the n.m.r. data obtained. The n.m.r. parameters are reported for the diastereomers L-alanyl-L or D-phenylalanine and L-phenylalanyl-L or D-alanine and for the dipeptide glycyl-L-phenylalanine and their carbamates. The results are interpreted in terms of preferred rotamers about the C.-CD bond of the phenylalanine residue and a p-type conformation of the peptide chain, wherein the two a-protons lie in the plane of the amide bond. All observations are in agreement with a shorter end to end distance in L,D-compared with L,L-dipeptides.

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Section: Resultsmentioning

confidence: 93%

Peptide Conformations. I. Nuclear Magnetic Resonance Study of the Carbamate Reaction of Amino Acids and Peptides

Lemieux¹,

Barton²

1971

Can. J. Chem.

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“…With a few exceptions, acidic solvent systems have been employed. Higher R f values were observed for the LL/DD diastereomeric pairs of free dipeptides than for the corresponding LD/DL epimers on cellulose, (29) silica gel, (29,34) and RP materials. (30) In contrast, AWP as adsorbent retained the LL/DD epimers more strongly than the LD/LD diastereomers, resulting in a reversal of the R f sequence.…”

Section: Thin-layer Chromatographymentioning

confidence: 96%

“…Separations of diastereomeric di-and tripeptides as free (29,30) or protected derivatives (31 -33) by TLC have been achieved using cellulose, (29) silica gel, (29,33,34) reversed-phase (RP) materials, (30) and RP phases impregnated with cationic or anionic detergents (30) or ammonium tungstophosphate (AWP)-coated plates (30) as stationary phases (Table 2). With a few exceptions, acidic solvent systems have been employed.…”

Section: Thin-layer Chromatographymentioning

confidence: 99%

Separation of Peptide Diastereomers

Scriba

2014

Encyclopedia of Analytical Chemistry

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Diastereomeric peptides, isomers in which one or more of the chiral centers have been converted to the opposite configuration (R or S, D or L ), often possess different biological activities and/or conformational properties. Therefore, the separation and determination of diastereomeric peptides is important in life sciences and particularly significant to the pharmaceutical industry for quality control of peptide synthesis and stability as well as for regulatory requirements. Diastereomers differ in their physicochemical properties that can be utilized for their determination by numerous techniques. In contrast to many other methods such as optical rotation, circular dichroism, differential scanning calorimetry, or infrared (IR) spectroscopy, separation techniques such as chromatography or capillary electrophoresis (CE) allow the sensitive and simultaneous identification and quantification of peptide diastereomers. This chapter covers analytical‐scale separation of peptide diastereomers by chromatographic methods, including paper chromatography (PC), thin‐layer chromatography (TLC), gas chromatography (GC), high‐performance liquid chromatography (HPLC), and CE. HPLC is currently the predominantly used method for peptide diastereomer separations. However, owing to the high resolving power, particularly for polar compounds, CE has been applied to the separation of diastereomeric peptides in recent years. The chapter focuses on methods employing achiral stationary phases or buffers without chiral additives for the separations, although some examples of such separations, i.e. the use of chiral columns or chiral mobile phase additives, are mentioned. Moreover, only diasteromeric peptides containing natural amino acids will be discussed.

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“…Scanning of the chromatograms is made by flame ionization detection in an Iatron TH-10 analyzer (Mills et al, 1979). Several workers (Pravda et al, 1964;Taschner et al, 1968;Wieland and Bende, 1965) have used silica plates for successful separation of dipeptide diastereoisomers, either as free peptides or the N-protected methyl esters. Qnly a few studies on the chromatography of diastereoisomeric tripeptides have been described in the literature (Sachs and Brand, 1959).…”

Section: Tlc On Silica Gel Layersmentioning

confidence: 99%