RYH: A minimal peptidic sequence obtained from beta-chain hemoglobin exhibiting an antimicrobial activity

Catiau, Lucie; Traisnel, Johnatan; Chihib, Nour‐Eddine; Flem, Guillaume Le; Blanpain, Annick; Melnyk, Oleg; Guillochon, Didier; Nedjar‐Arroume, Naïma

doi:10.1016/j.peptides.2011.05.021

Cited by 33 publications

(21 citation statements)

References 22 publications

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“…Lopes and others () have shown both the important role of tyrosine (Y) in the interaction with membranes, and the 2 positively charged amino acids, arginine and lysine, which interact with negatively charged membrane phospholipids. Recent results from Catiau and others () showed that the peptide β114 to 145 and its peptic derivatives containing the sequence RYH exhibited antibacterial activity. RYH was then chemically synthesized because hydrolysis did not result in this sequence.…”

Section: Bioactives Isolated From Animal Bloodmentioning

confidence: 99%

“…Comparing the KYR sequence with the sequence RYH obtained from the β‐chain of hemoglobin, both sequences contain tyrosine and 2 positively charged basic amino acids, including arginine. The authors concluded that tyrosine (Y), arginine (R), and one positively charged basic amino acid such as lysine (K) or histidine (H) are required for antibacterial activity (Catiau and others ). However, other peptides from bovine hemoglobin, which do not contain tyrosine or arginine (Froidevaux and others ; Hu and others ) still demonstrate antimicrobial activity, suggesting another mechanism of action.…”

Section: Bioactives Isolated From Animal Bloodmentioning

confidence: 99%

See 1 more Smart Citation

Slaughterhouse Blood: An Emerging Source of Bioactive Compounds

Bah

Bekhit

Carne

et al. 2013

Comp Rev Food Sci Food Safe

215

142

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Slaughterhouse blood is an inevitable part of the meat production food chain and represents a rich source of protein. The physicochemical characteristics and utilization of animal blood in various food and industrial applications has been well explored. However, in recent years much attention has been paid to the generation of peptides with biological activities from food by-products including blood. This review examines the angiotensin-converting enzyme inhibitory, antioxidant, antimicrobial, and other bioactive peptides derived from various slaughterhouse animal blood sources. Furthermore, the effect of enzyme choice, degree of hydrolysis, and peptide sequence or size on the potency of these bioactivity is discussed.

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Section: Bioactives Isolated From Animal Bloodmentioning

confidence: 99%

Section: Bioactives Isolated From Animal Bloodmentioning

confidence: 99%

Slaughterhouse Blood: An Emerging Source of Bioactive Compounds

Bah

Bekhit

Carne

et al. 2013

Comp Rev Food Sci Food Safe

215

142

View full text Add to dashboard Cite

show abstract

“…A number of bioactive peptides released from bovine hemoglobin hydrolysates have been reported. [29–32] It is a highly desirable but difficult task to identify bovine blood derived peptides. In this aspect, prediction model would be a useful technique to highlight potential ACE-inhibitory peptides identification.…”

Section: Introductionmentioning

confidence: 99%

Activity Prediction and Molecular Mechanism of Bovine Blood Derived Angiotensin I-Converting Enzyme Inhibitory Peptides

Zhang

Nie

et al. 2015

PLoS ONE

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Development of angiotensin I-converting enzyme (ACE, EC 3.4.15.1) inhibitory peptides from food protein is under extensive research as alternative for the prevention of hypertension. However, it is difficult to identify peptides released from food sources. To accelerate the progress of peptide identification, a three layer back propagation neural network model was established to predict the ACE-inhibitory activity of pentapeptides derived from bovine hemoglobin by simulated enzyme digestion. The pentapeptide WTQRF has the best predicted value with experimental IC50 23.93 μM. The potential molecular mechanism of the WTQRF / ACE interaction was investigated by flexible docking.

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“…Nonetheless, the blood of slaughtered animals is a potential source of bioactive peptides. Indeed, few publications have reported that the blood proteins, especially HB, are potential sources of bioactive peptides . Bovine HB is a protein easily digestible by the human GI digestion process.…”

Section: Discussionmentioning

confidence: 99%

Food peptidomics of in vitro gastrointestinal digestions of partially purified bovine hemoglobin: low‐resolution versus high‐resolution LC‐MS/MS analyses

et al. 2016

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Consumers and governments have become aware how the daily diet may affect the human health. All proteins from both plant and animal origins are potential sources of a wide range of bioactive peptides and the large majority of those display health-promoting effects. In the meat production food chain, the slaughterhouse blood is an inevitable co-product and, today, the blood proteins remain underexploited despite their bioactive potentiality. Through a comparative food peptidomics approach we illustrate the impact of resolving power, accuracy, sensitivity, and acquisition speed of low-resolution (LR)- and high-resolution (HR)-LC-ESI-MS/MS on the obtained peptide mappings and discuss the limitations of MS-based peptidomics. From in vitro gastrointestinal digestions of partially purified bovine hemoglobin, we have established the peptide maps of each hemoglobin chain. LR technique (normal bore C18 LC-LR-ESI-MS/MS) allows us to identify without ambiguity 75 unique peptides while the HR approach (nano bore C18 LC-HR-ESI-MS/MS) unambiguously identify more than 950 unique peptides (post-translational modifications included). Herein, the food peptidomics approach using the most performant separation methods and mass spectrometers with high-resolution capabilities appears as a promising source of information to assess the health potentiality of proteins.

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RYH: A minimal peptidic sequence obtained from beta-chain hemoglobin exhibiting an antimicrobial activity

Cited by 33 publications

References 22 publications

Slaughterhouse Blood: An Emerging Source of Bioactive Compounds

Slaughterhouse Blood: An Emerging Source of Bioactive Compounds

Activity Prediction and Molecular Mechanism of Bovine Blood Derived Angiotensin I-Converting Enzyme Inhibitory Peptides

Food peptidomics of in vitro gastrointestinal digestions of partially purified bovine hemoglobin: low‐resolution versus high‐resolution LC‐MS/MS analyses

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