scholarly journals Recent Advances in Chiral Analysis of Proteins and Peptides

Separations ◽  
2021 ◽  
Vol 8 (8) ◽  
pp. 112
Author(s):  
Marine Morvan ◽  
Ivan Mikšík
Keyword(s):  
Amino Acids ◽  
Stationary Phases ◽  
Enzymatic Digestion ◽  
Chiral Separations ◽  
Biological Compounds ◽  
Health And Disease ◽  
Electrophoretic Techniques ◽  
A Site ◽  
Future Work ◽  
Proteins And Peptides

Like many biological compounds, proteins are found primarily in their homochiral form. However, homochirality is not guaranteed throughout life. Determining their chiral proteinogenic sequence is a complex analytical challenge. This is because certain D-amino acids contained in proteins play a role in human health and disease. This is the case, for example, with D-Asp in elastin, β-amyloid and α-crystallin which, respectively, have an action on arteriosclerosis, Alzheimer's disease and cataracts. Sequence-dependent and sequence-independent are the two strategies for detecting the presence and position of D-amino acids in proteins. These methods rely on enzymatic digestion by a site-specific enzyme and acid hydrolysis in a deuterium or tritium environment to limit the natural racemization of amino acids. In this review, chromatographic and electrophoretic techniques, such as LC, SFC, GC and CE, will be recently developed (2018–2020) for the enantioseparation of amino acids and peptides. For future work, the discovery and development of new chiral stationary phases and derivatization reagents could increase the resolution of chiral separations.

scholarly journals In Vivo Identification of Intermediate Stages of the DNA Inversion Reaction Catalyzed by the Salmonella Hin Recombinase

Genetics ◽  
1998 ◽  
Vol 149 (4) ◽  
pp. 1649-1663
Author(s):  
Oliver Z Nanassy ◽  
Kelly T Hughes
Keyword(s):  
Amino Acids ◽  
Biochemical Analysis ◽  
Mutational Analysis ◽  
Recombination Reaction ◽  
Recombination Site ◽  
Dna Inversion ◽  
Hin Recombinase ◽  
One Step ◽  
A Site

Abstract The Hin recombinase catalyzes a site-specific recombination reaction that results in the reversible inversion of a 1-kbp segment of the Salmonella chromosome. The DNA inversion reaction catalyzed by the Salmonella Hin recombinase is a dynamic process proceeding through many intermediate stages, requiring multiple DNA sites and the Fis accessory protein. Biochemical analysis of this reaction has identified intermediate steps in the inversion reaction but has not yet revealed the process by which transition from one step to another occurs. Because transition from one reaction step to another proceeds through interactions between specific amino acids, and between amino acids and DNA bases, it is possible to study these transitions through mutational analysis of the proteins involved. We isolated a large number of mutants in the Hin recombinase that failed to carry out the DNA exchange reaction. We generated genetic tools that allowed the assignment of these mutants to specific transition steps in the recombination reaction. This genetic analysis, combined with further biochemical analysis, allowed us to define contributions by specific amino acids to individual steps in the DNA inversion reaction. Evidence is also presented in support of a model that Fis protein enhances the binding of Hin to the hixR recombination site. These studies identified regions within the Hin recombinase involved in specific transition steps of the reaction and provided new insights into the molecular details of the reaction mechanism.

PAPER CHROMATOGRAPHY OF COMPLEX BIOLOGICAL MATERIALS BY SOLVENT REDEVELOPMENT WITHOUT PRIOR REMOVAL OF SALTS OR PROTEINS

1960 ◽  
Vol 38 (10) ◽  
pp. 1137-1147 ◽  
Author(s):  
Arthur E. Pasieka
Keyword(s):  
Amino Acids ◽  
Paper Chromatography ◽  
Filter Paper ◽  
Complex Mixtures ◽  
Two Dimensional ◽  
One Dimensional ◽  
Equivalent Time ◽  
Biological Compounds ◽  
High Concentrations ◽  
Subsequent Staining

A solvent redeveloping technique has been devised by which amino acids, peptides, and sugars can be separated from complex mixtures in the presence of high concentrations of salts and proteins. The separations are effected by two to four successive 18-hour solvent developments with drying between each 18-hour period before subsequent staining of the chromatograms. Better separations and resolutions are obtained by such successive 18-hour solvent developments than by one continuous solvent development for an equivalent time. The effect of these redevelopments on the separations and resolutions of biological compounds is illustrated at various stages by photographs of one- and two-dimensional chromatograms. The redevelopment technique requires filter paper sheets up to 4 ft in length for one-dimensional analytical and preparative types of chromatograms.

Interactions of mouse glycophorin A with the dRTA-related mutant G719D of the mouse Cl–/HCO3– exchanger Ae1This paper is one of a selection of papers published in a Special Issue entitled CSBMCB 53rd Annual Meeting — Membrane Proteins in Health and Disease, and has undergone the Journal’s usual peer review process.

2011 ◽  
Vol 89 (2) ◽  
pp. 224-235 ◽  
Author(s):  
Andrew K. Stewart ◽  
Fouad T. Chebib ◽  
Syed W. Akbar ◽  
Maria J. Salas ◽  
Rajan A. Sonik ◽  
...  
Keyword(s):  
Amino Acids ◽  
Transmembrane Domain ◽  
Peer Review Process ◽  
Surface Expression ◽  
Amino Acid Sequences ◽  
Glycophorin A ◽  
Specific Expression ◽  
Health And Disease ◽  
Renal Tubular

The AE1 mutation G701D, associated with recessive distal renal tubular acidosis (dRTA), produces only minimal erythroid phenotype, reflecting erythroid-specific expression of stimulatory AE1 subunit glycophorin A (GPA). GPA transgene expression could theoretically treat recessive dRTA in patients and in mice expressing cognate Ae1 mutation G719D. However, human (h) GPA and mouse (m) Gpa amino acid sequences are widely divergent, and mGpa function in vitro has not been investigated. We therefore studied in Xenopus oocytes the effects of coexpressed mGpa and hGPA on anion transport by erythroid (e) and kidney (k) isoforms of wild-type mAe1 (meAe1, mkAe1) and of mAe1 mutant G719D. Coexpression of hGPA or mGpa enhanced the function of meAe1 and mkAe1 and rescued the nonfunctional meAe1 and mkAe1 G719D mutants through increased surface expression. Progressive N-terminal truncation studies revealed a role for meAe1 amino acids 22–28 in GPA-responsiveness of meAe1 G719D. MouseN-cyto/humanTMD and humanN-cyto/mouseTMD kAE1 chimeras were active and GPA-responsive. In contrast, whereas chimera mkAe1N-cyto/hkAE1 G701DTMD was GPA-responsive, chimera hkAE1N-cyto/mkAe1 G719DTMD was GPA-insensitive. Moreover, whereas the isolated transmembrane domain (TMD) of hAE1 G701D was GPA-responsive, that of mAe1 G719D was GPA-insensitive. Thus, mGpa increases surface expression and activity of meAe1 and mkAe1. However, the G719D mutation renders certain mAe1 mutant constructs GPA-unresponsive and highlights a role for erythroid-specific meAe1 amino acids 22–28 in GPA-responsiveness.

NonO, a non-POU-domain-containing, octamer-binding protein, is the mammalian homolog of Drosophila nonAdiss

1993 ◽  
Vol 13 (9) ◽  
pp. 5593-5603
Author(s):  
Y S Yang ◽  
J H Hanke ◽  
L Carayannopoulos ◽  
C M Craft ◽  
J D Capra ◽  
...  
Keyword(s):  
Amino Acids ◽  
Dna Binding ◽  
Protein Binding ◽  
Aromatic Amino Acids ◽  
Courtship Song ◽  
Dna Binding Domain ◽  
Binding Motifs ◽  
Dna And Rna ◽  
Pou Domain ◽  
A Site

We have cloned the ubiquitous form of an octamer-binding, 60-kDa protein (NonO) that appears to be the mammalian equivalent of the Drosophila visual and courtship song behavior protein, no-on-transient A/dissonance (nonAdiss). A region unprecedently rich in aromatic amino acids containing two ribonuclear protein binding motifs is highly conserved between the two proteins. A ubiquitous form of NonO is present in all adult tissues, whereas lymphocytes and retina express unique forms of NonO mRNA. The ubiquitous form contains a potential helix-turn-helix motif followed by a highly charged region but differs from prototypic octamer-binding factors by lacking the POU DNA-binding domain. In addition to its conventional octamer duplex-binding, NonO binds single-stranded DNA and RNA at a site independent of the duplex site.

Chiral separations of metoprolol and some analogs with carbon dioxide on chiralcel OD and chiralpak AD stationary phases. Use of chemometrics

2000 ◽  
Vol 51 (5-6) ◽  
pp. 283-293 ◽  
Author(s):  
S. Svensson ◽  
A. Karlsson ◽  
O. Gyllenhaal ◽  
J. Vessman
Keyword(s):  
Carbon Dioxide ◽  
Stationary Phases ◽  
Chiral Separations ◽  
Chiralcel Od

Influence of silica functionalization by amino acids and peptides on the stationary phases zeta potential

2018 ◽  
Vol 1573 ◽  
pp. 98-106 ◽  
Author(s):  
Magdalena Skoczylas ◽  
Szymon Bocian ◽  
Bogusław Buszewski
Keyword(s):  
Amino Acids ◽  
Zeta Potential ◽  
Stationary Phases

High–throughput enantioseparation of Nα–fluorenylmethoxycarbonyl proteinogenic amino acids through fast chiral chromatography on zwitterionic-teicoplanin stationary phases

2020 ◽  
Vol 1624 ◽  
pp. 461235
Author(s):  
Giulia Mazzoccanti ◽  
Simone Manetto ◽  
Antonio Ricci ◽  
Walter Cabri ◽  
Andrea Orlandin ◽  
...  
Keyword(s):  
Amino Acids ◽  
High Throughput ◽  
Stationary Phases ◽  
Chiral Chromatography
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