Biomedical applications of dipeptides and tripeptides

Santos, Sara; Torcato, Inês M.; Castanho, Miguel A. R. B.

doi:10.1002/bip.22067

Cited by 54 publications

(42 citation statements)

References 58 publications

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“…Both have several putative glycosylation phosphorylation sites, and it has been suggested that these transporters are constituted by 12 transmembrane domains, with both the C-and N-terminal localized inside the cell. Di-peptides/tri-peptides and peptide-mimetic drug molecules resistant to enzymatic degradation in the cytosol are suggested to be transported by a saturable transport system that is yet to be identified [51].…”

Section: Peasmentioning

confidence: 99%

Bioactive Peptides from Legumes as Anticancer Therapeutic Agents

González-Montoya¹

2017

Int J Cancer Clin Res

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Food proteins are a source of nutraceutical and bioactive peptides that promote health and prevent diseases. Legume seed proteins have been widely studied to produce peptides (protein fragments) with a diversity of biological activities. Generally, these Bioactive Peptides (BPs) are encrypted in proteins but can be released by modifications or cleavage from original protein by means of enzymes during gastrointestinal transit or processes as fermentation, germination, heating and pressure. Storage proteins, lectins and protease inhibitors have been reported to be sources of BPs. These peptides are capable of generating a physiological effect against cancer cells and can induce cell death by different mechanisms like apoptosis, affecting the tubulin-microtubule equilibrium and inhibiting angiogenesis. Finally, anticancer therapy based on legume-derived peptides could play a significant role in the pharmaceutical and nutraceutical industry due to the benefits as functional ingredients which improve the life quality of patients or reduce the risk of cancer.

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Section: Peasmentioning

confidence: 99%

Bioactive Peptides from Legumes as Anticancer Therapeutic Agents

González-Montoya¹

2017

Int J Cancer Clin Res

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“…In recent years, research on cyanophycin (multi‐ l ‐arginyl‐poly‐[ l ‐aspartic acid], CGP) is not only solely focusing on aspects of fundamental research, but also more application‐oriented aspects are investigated. Large‐scale production of CGP was established; new purification methods have been developed; and applications for CGP and its dipeptides are entering commercial use . These applications include the use of the CGP molecule as precursor for the synthesis of polyaspartic acid and the possible use of CGP dipeptides in areas like peptide‐based diets in clinical fields or as dietary supplement and in the feed of life stock …”

Section: Introductionmentioning

confidence: 99%

“…

possible use of CGP dipeptides in areas like peptide-based diets in clinical fi elds or as dietary supplement [ 6 ] and in the feed of life stock. [ 4 ] An important part of CGP research focusses on the development of novel variants of CGP, both in its composition and in its characteristics. Alternative constituents can be generated by several different strains that synthesize CGP with relevant amounts of lysine, [ 7 ] ornithine, [ 8 ] or citrulline [ 8,9 ] replacing the arginine side-chains.

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mentioning

confidence: 99%

Enzymatic Modification of Soluble Cyanophycin Using the Type II Peptidyl Arginine Deiminase from Oryctolagus cuniculus

Wiefel

Steinbüchel

2016

Macromolecular Bioscience

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An increased structural variety expands the number of putative applications for cyanophycin (multi-l-arginyl-poly-[l-aspartic acid], CGP). Therefore, structural modifications of CGP are of major interest; these are commonly obtained by modification and optimization of the bacterial producing strain or by chemical modification. In this study, an enzymatic modification of arginine side chains from lysine-rich CGP is demonstrated using the peptidyl arginine deiminase from Oryctolagus cuniculus, purified from Escherichia coli after heterologous expression. About 10% of the arginine side chains are converted to citrulline which corresponds to 4% of the polymer's total side chains. An inhibition of the reaction in the presence of small amounts of l-citrulline is observed, thereby explaining the low conversion rate. CGP dipeptides can be modified with about 7.5 mol% of the Asp-Arg dipeptides being converted to Asp-Cit. These results show that the enzymatic modification of CGP is feasible, opening up a whole new area of possible CGP modifications for further research.

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“…phaseolicola 1448A (Arai & Kino, 2008;Bender et al, 1999) and TabS from P. syringae 14081 (Arai et al, 2013). LALs are potentially useful for the industrial production of antibiotics, phytotoxins and other medical and healthcarerelated peptides (Yagasaki & Hashimoto, 2008;Mills et al, 2011;Santos et al, 2012). For example, BacD is involved in the biosynthesis of the antibiotic bacilysin and is utilized in the industrial production of alanyl-glutamine, which is an important component of parenteral nutrition.…”

Section: Introductionmentioning

confidence: 99%