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Current Molecular Medicine

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ISSN (Print): 1566-5240
ISSN (Online): 1875-5666

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Review Article

The Antihypertensive, Antimicrobial and Anticancer Peptides from Arthrospira with Therapeutic Potential: A Mini Review

Author(s): Grecia E. Barriga Montalvo, Luciana Porto de Souza Vandenberghe , Vanete Thomaz Soccol, Júlio Cesar de Carvalho and Carlos Ricardo Soccol*

Volume 20, Issue 8, 2020

Page: [593 - 606] Pages: 14

DOI: 10.2174/1566524020666200319113006

Price: $65

Abstract

The interest in biological peptides from Arthrospira sp. (syn Spirulina) is increasing due to its Generally Recognised as Safe “GRAS” status, the high concentration of proteins and the history of its use as a supplement and nutraceutical agent. Arthrospira peptides can be generated by the controlled hydrolysis of proteins, using proteases, followed by fractionation. The peptides obtained have a range of therapeutic effects. Amongst these bioactive peptides, three classes are of major importance: the antihypertensive (AHP), antimicrobial (AMP) and anticancer (ACP) peptides. AHPs have the ability to work as inhibitors of angiotensin-converting enzyme (ACE), and help to control several diseases such as hypertension, obesity, and cardiovascular issues, AMPs play a crucial role in the immune response, inhibiting the development of pathogens such as bacteria, fungi, viruses and others, while ACPs can aid in tumour control by the induction of apoptosis or necrosis, or the inhibition of angiogenesis. Thus, bioactive peptides are of great significance to the pharmaceutical industry. However, they can show secondary effects. This paper reviews the inhibition mechanism of antimicrobial, hypertensive and anticancer peptides from Arthrospira sp., and the possible structures of the peptides according to the type of activity and its intensity. In addition, this paper describes the purification methods of absorption mechanisms, and reviews databases for designing peptides.

Keywords: Spirulina, bioactive peptides, antihypertensive, antimicrobial, anticancer, enzymatic hydrolysis.

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