On the spontaneous abiotic peptization of phenylglycine in an aqueous medium

Sajewicz, Mieczysław; Gontarska, Monika; Kronenbach, Dorota; Kowalska, Teresa

doi:10.1556/achrom.21.2009.1.13

Cited by 15 publications

(31 citation statements)

References 10 publications

(9 reference statements)

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“…The results of the biuret test performed with S-, R-, and rac-phenylglycine [16] also indicate the presence of oligopeptides in aged samples.…”

Section: S-phenylglycinementioning

confidence: 85%

“…Based on the results of biuret test [16], it seems that oligopeptides are the most probable outcome of this process. We compare the chromatograms of the freshly prepared S-phenylglycine solution with those stored for nine days and for one year (Fig.…”

Section: S-phenylglycinementioning

confidence: 99%

“…In subsequent papers [16][17][18], we demonstrated via the biuret test [16] and 13 C NMR spectroscopy [17,18] that profens, amino acids, and hydroxy acids can also undergo spontaneous condensation or peptidization when stored for sufficient time in 70% aqueous ethanol.…”

Section: Introductionmentioning

confidence: 98%

“…There are several analogies between the results presented in their studies and those found in our own laboratory, which have inspired us to focus on the dynamics of condensation or peptidization of chiral low-molecular-weight carboxylic acids. For this reason, and because of the potential importance of this process in synthetic biology and chemical evolution, we have decided to focus on the issue of peptidization of amino acids coupled to their oscillatory chiral conversion [16]. More specifically, we scrutinize here the dynamics of peptidization of the low-molecular-weight amino acids, R-, S-, and rac-phenylglycine.…”

Section: Introductionmentioning

confidence: 99%

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Condensation oscillations in the peptidization of phenylglycine

et al. 2010

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In earlier studies, we showed that certain low-molecular-weight carboxylic acids (profens, amino acids, hydroxy acids) can undergo spontaneous in vitro chiral conversion accompanied by condensation to from oligomers, and we proposed two simple models to describe these processes. Here, we present the results of investigations using non-chiral high-performance liquid chromatography with diode array detector (HPLC-DAD) and mass spectrometry (MS) on the dynamics of peptidization of S-, R-, and rac-phenylglycine dissolved in 70% aqueous ethanol and stored for times up to one year. The experimental results demonstrate that peptidization of phenylglycine can occur in an oscillatory fashion. We also describe, and carry out simulations with, three models that capture key aspects of the oscillatory condensation and chiral conversion processes.

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“…The results of the biuret test performed with S-, R-, and rac-phenylglycine [16] also indicate the presence of oligopeptides in aged samples.…”

Section: S-phenylglycinementioning

confidence: 85%

Section: S-phenylglycinementioning

confidence: 99%

Section: Introductionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

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Condensation oscillations in the peptidization of phenylglycine

et al. 2010

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“…5 [27]. Similarly, spontaneous peptidization of phenylglycine dissolved in 70% aqueous ethanol (and in dichloromethane) was confirmed by a simple biuret test [29]. Thus it became evident that spontaneous condensation (or peptidization) is most probably inherent in all chiral low-molecular-weight carboxylic acids and it probably runs in parallel with the oscillatory chiral conversion.…”

Section: Spontaneous Oscillatory Condensation Of Profens Through the mentioning

confidence: 95%

On ups and downs by analysis of profen drugs. A mini review

Sajewicz

Kowalska

2012

Acta Chromatographica

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Summary. Drug analysis is among the most sensitive areas of chemical analysis, simply because of its relevance to human health. Profens make the most important group of nonsteroidal anti-inflammatory drugs (NSAIDs), and in many countries some of them are freely sold over the counter. The in vitro liquid chromatographic analysis of profen drugs faces certain not commonly recognized yet acute and often impassable problems, due to the specific physicochemical properties of these compounds. In this mini review, we share our experience on the practical failures with the enantioseparation of profen drugs both by means of chiral planar and column chromatography. By use of such analytical techniques as polarimetry, 1 H and 13 C NMR spectroscopy, and mass spectrometry, we point out objectively the reasons that make liquid chromatographic enantioseparation of profens an almost impossible task. These compounds have an inherent ability (both in aqueous and nonaqueous solutions) to undergo oscillatory chiral conversion and oscillatory condensation, combined with a highly pronounced gelating ability. In our view, the oscillatory chiral conversion of profens questions the credibility of widespread claims on the superiority of the curative potential with the (+)-profens over that of the respective (-)-antimers (although the rightfulness of such claims cannot be dismissed, as the in vivo and in vitro behavior of many drugs are known to sometimes fundamentally differ). Moreover, it seems highly probable that, due to their highly pronounced gelating property, profen drugs can easily clog the blood vessels and thereby jeopardize living organisms.

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Scanning Electron Microscopic Evidence of Spontaneous Heteropeptide Formation in Abiotic Solutions of Selected α‐Amino Acid Pairs

Godziek

Maciejowska

Talik

et al. 2016

Israel Journal of Chemistry

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Spontaneous nonlinear peptidization of the monomeric and enantiomerically pure α‐amino acids in abiotic aqueous and nonaqueous solutions is still regarded by some as a somewhat puzzling phenomenon, and therefore it needs additional experimental authentication. In our earlier studies, we employed several analytical techniques to prove its occurrence. In this study, we present the scanning electron microscopic (SEM) evidence of spontaneous heteropeptide formation in the binary L‐Cys−L‐Phe, L‐Cys−L‐Phg, and L‐Cys−L‐Pro mixtures dissolved in 70 % aqueous methanol. With each α‐amino acid pair, one amino acid (L‐Cys) is equipped with three functionalities (−SH, −NH2, and −COOH), enabling formation of the spherical homopeptide microstructures, while its counterpart (L‐Phe, L‐Phg, or L‐Pro, respectively) is equipped with the two functionalities only (−NH2 or =NH, and −COOH). The SEM micrographs of the peptidization products originating from the three investigated α‐amino acid pairs show three different, yet spherical, structures, which seem suggestive of the heteropeptide formation involving both L‐Cys and its counterpart α‐amino acid. Additional confirmation of heteropeptide formation is furnished by high performance liquid chromatography (HPLC), the biuret test, and mass spectrometry (MS).

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On the spontaneous abiotic peptization of phenylglycine in an aqueous medium

Cited by 15 publications

References 10 publications

Condensation oscillations in the peptidization of phenylglycine

Condensation oscillations in the peptidization of phenylglycine

On ups and downs by analysis of profen drugs. A mini review

Scanning Electron Microscopic Evidence of Spontaneous Heteropeptide Formation in Abiotic Solutions of Selected α‐Amino Acid Pairs

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