Inferring Peptide Composition from Molecular Formulas

Author(s):  
Sebastian Böcker ◽  
Anton Pervukhin
Keyword(s):  
2020 ◽  
Vol 4 (1) ◽  
Author(s):  
Paulus G. M. Jochems ◽  
Willem R. Keusters ◽  
Antoine H. P. America ◽  
Pascale C. S. Rietveld ◽  
Shanna Bastiaan-Net ◽  
...  

AbstractFood security is under increased pressure due to the ever-growing world population. To tackle this, alternative protein sources need to be evaluated for nutritional value, which requires information on digesta peptide composition in comparison to established protein sources and coupling to biological parameters. Here, a combined experimental and computational approach is presented, which compared seventeen protein sources with cow’s whey protein concentrate (WPC) as the benchmark. In vitro digestion of proteins was followed by proteomics analysis and statistical model-based clustering. Information on digesta peptide composition resulted in 3 cluster groups, primarily driven by the peptide overlap with the benchmark protein WPC. Functional protein data was then incorporated in the computational model after evaluating the effects of eighteen protein digests on intestinal barrier integrity, viability, brush border enzyme activity, and immune parameters using a bioengineered intestine as microphysiological gut system. This resulted in 6 cluster groups. Biological clustering was driven by viability, brush border enzyme activity, and significant differences in immune parameters. Finally, a combination of proteomic and biological efficacy data resulted in 5 clusters groups, driven by a combination of digesta peptide composition and biological effects. The key finding of our holistic approach is that protein source (animal, plant or alternative derived) is not a driving force behind the delivery of bioactive peptides and their biological efficacy.


1997 ◽  
Vol 41 (3) ◽  
pp. 504-510 ◽  
Author(s):  
A Severin ◽  
E Severina ◽  
A Tomasz

Subinhibitory concentrations of clavulanate caused premature induction of stationary-phase autolysis, sensitization to lysozyme, and reductions in the MICs of deoxycholate and penicillin for Streptococcus pneumoniae. In the range of clavulanate concentrations producing these effects, this beta-lactam compound was selectively bound to PBP 3. Cell walls isolated from pneumococci grown in the presence of clavulanate showed increased sensitivity to the hydrolytic action of purified pneumococcal autolysin in vitro. High-performance liquid chromatography analysis of the peptidoglycan isolated from the clavulanate-grown cells showed major qualitative and quantitative changes in stem peptide composition, the most striking feature of which was the accumulation of peptide species carrying intact D-alanyl-D-alanine residues at the carboxy termini. The altered biological and biochemical properties of the clavulanate-grown pneumococci appear to be the consequences of suppressed D,D-carboxypeptidase activity.


1977 ◽  
Vol 55 (7) ◽  
pp. 766-768 ◽  
Author(s):  
Bernard Rubenstein ◽  
Susan Evans ◽  
George Steiner

We have devised a new method for the fractionation of human plasma high density lipoprotein (HDL). The HDL was chromatographed on DEAE-agarose columns using a continuous gradient of 0.06–0.15 M NaCl. The elution pattern obtained showed three phases, each with differing peptide composition. Examination of the three subfractions showed that each contained both apo A-I and apo A-II, but indifferent proportions. Subfraction 1 contained noapoC-II orC-III-1 and only a trace of apo C-III-2, subfraction 2 contained apo C-II and C-III-1 but no C-III-2, while subfraction 3 contained considerable apo C-III-2 with only traces of apo C-II or C-III-1.


2010 ◽  
Vol 121 (2) ◽  
pp. 457-467 ◽  
Author(s):  
Seronei Chelulei Cheison ◽  
Meike Schmitt ◽  
Elena Leeb ◽  
Thomas Letzel ◽  
Ulrich Kulozik

2009 ◽  
Vol 423 (3) ◽  
pp. 353-361 ◽  
Author(s):  
Kurt H. Piepenbrink ◽  
Oleg Y. Borbulevych ◽  
Ruth F. Sommese ◽  
John Clemens ◽  
Kathryn M. Armstrong ◽  
...  

TCR (T-cell receptor) recognition of antigenic peptides bound and presented by MHC (major histocompatibility complex) molecules forms the basis of the cellular immune response to pathogens and cancer. TCRs bind peptide–MHC complexes weakly and with fast kinetics, features which have hindered detailed biophysical studies of these interactions. Modified peptides resulting in enhanced TCR binding could help overcome these challenges. Furthermore, there is considerable interest in using modified peptides with enhanced TCR binding as the basis for clinical vaccines. In the present study, we examined how fluorine substitutions in an antigenic peptide can selectively impact TCR recognition. Using a structure-guided design approach, we found that fluorination of the Tax peptide [HTLV (human T-cell lymphotropic virus)-1 Tax11-19] enhanced binding by the Tax-specific TCR A6, yet weakened binding by the Tax-specific TCR B7. The changes in affinity were consistent with crystallographic structures and fluorine chemistry, and with the A6 TCR independent of other substitutions in the interface. Peptide fluorination thus provides a means to selectively modulate TCR binding affinity without significantly perturbing peptide composition or structure. Lastly, we probed the mechanism of fluorine's effect on TCR binding and we conclude that our results were most consistent with a ‘polar hydrophobicity’ mechanism, rather than a purely hydrophobic- or electrostatic-based mechanism. This finding should have an impact on other attempts to alter molecular recognition with fluorine.


2017 ◽  
Vol 97 ◽  
pp. 211-217 ◽  
Author(s):  
Valter H.M. Santos ◽  
Igor O. Minatel ◽  
Paulo C. Reco ◽  
Alexandre Garcia ◽  
Giuseppina P.P. Lima ◽  
...  

2019 ◽  
Vol 119 (8) ◽  
pp. 75 ◽  
Author(s):  
O. A. Gromova ◽  
I. Yu. Torshin ◽  
V. G. Zgoda ◽  
O. V. Tikhonova

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