A potent and novel anticoagulant peptide was enzymatically isolated from the edible seaweed Porphyra yezoensis (commercially known as Nori). The pepsin hydrolysate showed 35% degree of hydrolysis and exhibited higher anticoagulant activity than undigested crude. The hydrolysate was fractionated by 4 sequential steps using size exclusion on Sephadex G-100, anion exchange, Sephadex G25 chromatography and desalting by Sephadex G-10. The purified peptide showed a single peak on RP-HPLC. The molecular mass of the peptide obtained by MS/MS analysis was 1.77 kDa and its sequence was identified as NMEKGSSSVVSSRM(+15.99)KQ. In vitro anticoagulation assays of purified peptide for clotting time with human plasma showed a dose-dependent prolongation of activated partial thromboplastin time from normal 35 s to 320 s with IC50 value of 0.3 μM. It did not prolong prothrombin or thrombin time. These results emphasise that the peptide interacts with the clotting factors involved in the intrinsic pathway of coagulation. © 2015 Elsevier Ltd.

Alka Mehta

Department of Integrative Biology

School of Bio Sciences and Technology

Vellore Campus

Indumathi P

Vellore Institute of Technology (VIT) is a private university located in&nbsp;Tamil Nadu, India. Founded in 1984, as Vellore Engineering College, the institution offers 20 undergraduate, 34 postgraduate, four integrated and four research programs. It has campuses in Vellore, Amravati, Bhopal and Chennai.

VIT is one of the top ranked private universities in India according to NIRF, THE and QS Rankings.&nbsp;Govt. of India has recognized&nbsp;VIT, Vellore as an&nbsp;Institution of Eminence. This has allowed VIT to take independent quality initiatives and move up in world ranking.

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VIT University

Journal of Functional Foods

Porphyra, one of the most cultured red algae has gained economic importance across the globe for its nutritional benefits. Porphyra is being cultivated, harvested, dried, processed and consumed in large quantities in south eastern countries. It contains relatively high amounts of proteins, carbohydrates, and micronutrients. Exploitation of its fundamental attributes led to the discovery of various biologically active compounds like polysaccharides, phycobiliproteins and peptides with effective pharmacological applications. In this review, a systematic account of the research accomplished in the past decade and up-to-date overview of various bioactive compounds and its pharmacological implications has been compiled. This review summarizes the bioactivities like antioxidative, immunomodulatory, antihypertensive, anticoagulant and anticancer properties of the bioactive compounds from Porphyra.

Fulltext

Plant Foods for Human Nutrition

Health Benefits and Pharmacological Effects of Porphyra Species

Thrombosis represents a major cause of morbidity and mortality around the world. Peptides isolated from natural sources have been proven to have anticoagulant and antithrombotic properties. VITPOR AI, a 16-mer peptide, isolated from Porphyra yezoensis was reported to have anticoagulant property. In this study, the coagulation factor XIIa activity in the presence of VITPOR AI was determined. Molecular modelling was performed to investigate the interaction between peptide and FXIIa. The structure of the peptide was predicted using PEP-FOLD3 server and simulated by molecular dynamics (MD) using GROMACS package. Molecular docking was carried out using peptide-protein docking software, pepATTRACT and its stability was confirmed by MD simulations. The chromogenic substrate assay revealed that the peptide inhibited the amidolytic activity of FXIIa with IC 50 of 70.24 μM. The docking result showed peptide interactions through hydrogen bonds with Pro 96, Tyr 99, Glu 146, Gly 193 and Ser 195 of FXIIa. The MD simulation demonstrated that the peptide's binding with the FXIIa was stable as it did not move away from its binding region throughout the simulation period of 100 ns Moreover, MM/PBSA analysis also indicated a stable binding between the protein and peptide. These results suggest that the inhibition of the FXIIa activity might be due to binding of the peptide to oxyanion hole of the catalytic site. Thus, VITPOR AI could be explored as a potent anticoagulant which inhibits only intrinsic pathway of coagulation cascade but does not affect the extrinsic pathway. © 2019 Elsevier Inc.

Journal of Molecular Graphics and Modelling

An anticoagulant peptide from Porphyra yezoensis inhibits the activity of factor XIIa: In vitro and in silico analysis

Anticoagulant drugs are of crucial importance for the treatment and prophylaxis of thrombotic disorders. The use of traditional anticoagulants like heparin and warfarin is majorly associated with bleeding complications. In the quest for safer anticoagulation therapy, the interest for the isolation of novel anticoagulant compounds has shifted towards natural sources. Peptides can be considered as better alternative due to their therapeutic potential in the treatment of diseases. Peptides from hematophagous (blood-feeding) and venomous organisms have been recognized as potential anticoagulant agents. Of late, peptides derived from the hydrolysis of food proteins, including edible seaweeds, milk and seed proteins, have also shown to possess promising in vitro anticoagulant activity. To overcome the problems associated with regular anticoagulants, peptides targeting vital steps in the clotting cascade have been studied. This review focuses on anticoagulant peptides with known targets, inhibiting crucial factors in the coagulation cascade such as FXa, FXIa, FXIIa and FVIIa/TF complex, as well as peptides with unknown targets. © 2018, Springer Science+Business Media, LLC, part of Springer Nature.

International Journal of Peptide Research and Therapeutics

Target Specific Anticoagulant Peptides: A Review

The main aim of the review is to recapitulate the effects of thrombotic diseases, clotting disorders, and the methodology of prospecting a range of thrombolytics from various sources and thrombolytic therapies. Thrombolytic medications are administered to infringe dangerous clots inside blood vessels when there is deprivation in this haemostatic balance. Certain bioactive compounds present in herbs, plant leaves, roots and fruits exhibit thrombolytic activities. Serine proteases, metalloproteases and some cysteine proteases possess thrombolytic properties. These proteases are found in plants, humans, animals and microbes as well. Thrombolytics which are of clinical importance are discussed in this article along with its variants and biological sources exhibiting thrombolytic activity. Alternative therapies followed in recent days are also discussed, including future prospects of research on thrombolytics. Knowledge of thrombolytic biodiversity plays a decisive role in choosing safe, economic and effective thrombolytics for scale up and commercialization. © 2018, Institute of Korean Medicine, Kyung Hee University and Springer Science+Business Media B.V., part of Springer Nature.

Oriental Pharmacy and Experimental Medicine

Focalization of thrombosis and therapeutic perspectives: a memoir

Annals of Allergy, Asthma & Immunology

Author Index to Volume 116, 2016

Peptides

A novel peptide inhibitor of platelet aggregation from stiff silkworm, Bombyx batryticatus

Applied Biochemistry and Biotechnology

A Two-Step, One-Pot Enzymatic Method for Preparation of Duck Egg White Protein Hydrolysates with High Antioxidant Activity

Drug Development Research

Antithrombotic Therapy for Prevention of Various Thrombotic Diseases

Marine Proteins and Peptides

A novel anticoagulant peptide from the Nori hydrolysate

Journal	Data powered by TypesetJournal of Functional Foods
Publisher	Data powered by TypesetElsevier BV
ISSN	1756-4646
Open Access	0