New antibacterial peptide derived from bovine hemoglobin

Daoud, Rachid; Dubois, Véronique; Bors-Dodita, Loredana; Nedjar‐Arroume, Naïma; Krier, François; Chihib, Nour‐Eddine; Mary, P.; Kouach, Mostafa; Briand, Gilbert; Guillochon, Didier

doi:10.1016/j.peptides.2004.12.008

Cited by 116 publications

(79 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The ACE enzyme is found in various tissues and its inhibition can influence different systems involved in the regulation of blood pressure, in addition to the immune and nervous systems [22]. ACE inhibitors have been isolated from the primary sequences of αS1-casein (fs: 23-34; 23-27; 294-299), of bovine β-casein (f: 177-183), human (f: [43][44][45][46][47][48][49][50][51][52] and of kappa-casein (f: [63][64][65]. These peptides are generally called casokinins [23].…”

Section: Antihypertensive Peptidesmentioning

confidence: 99%

“…The following amino acid composition was established through the use of mass spectrometry: Val-Leu-Ser-Ala-Ala-Asp-Lys-Gly-Asn-Val-Lys-Ala-Ala-TrpGly-Lys-Val-Gly-Gly-His-Ala-Ala-Glu (MM 2,236.9Da). Activity was tested against growth of M. luteus A270 bacteria in liquid culture medium.A more recent research [46] submitted bovine hemoglobin to hydrolysis by pepsin (pH 4.5, 23 º C), isolating and purifying from the hydrolysate the peptide: Val-Thr-Leu-Ala-Ser-His-Leu-Pro-Ser-AspPhe-Thr-Pro-Ala-Val-His-Ala-Ser-Leu-Asp-Lys-Phe-Leu-Ala-AsnVal-Ser-Thr-Val-Leu (MM 3.150Da). Antimicrobial activity was tested against 9 lineages: 3 Gram (-) lineages, Escherichia coli, Shigiella sonnei, and Salmonella enteritidis; 6 Gram (+) lineages, M. luteus A270, Listeria innocua, Enterococcus faecalis, Bacillus cereus, Staphylococcus saprophyticus, and Staphylococcus similans.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Food Proteins and Bioactive Peptides, Functional Diets

Sgarbieri¹,

Armadas²

2017

FSN

View full text Add to dashboard Cite

Throughout the second half of the last century and early this century the concept of the biological function of food proteins has changed significantly. While in the past the food proteins were regarded only as macronutrients capable of providing the amino acids to form the protein component of organs and tissues, also participating in the generation of metabolic energy for the normal functioning of living organisms, today it is known that certain proteins present in food, as well as fragments or peptides derived thereof, may participate in the general metabolism in a much more interactive manner, through bioactivities that go far beyond the nutritional functions that had been established by the end of the first half of the prior century.By making an analogy with the aeronautical activity we can say that in the past the food proteins functioned as black boxes holding numerous important pieces of information, which research and technology have only revealed, in part, in recent decades. In this period it Received: August 07, 2017; Accepted: September 12, 2017; Published: September 26, 2017 was found that certain proteins present in foods are naturally bioactive, and can be absorbed from the Gastrointestinal System (GIS) in their intact or slightly modified form and exercise specific bioactivities in the systemic metabolism [1], or, in addition, resist the action of digestive enzymes exercising different bioactivities in the gastrointestinal system [2]. Even more interesting were the findings that food proteins, of both plant and animal origin, contain, in their primary structures, specific amino acid sequences in their polypeptide chains, which when cleaved in the form of peptides by proteolytic enzymes or by specific chemical reagents may exercise diverse bioactivities that were latent in the original structure of the protein from which they originated.Bioactive peptides have been obtained from precursor proteins through the use of methodologies that have reached a high degree of sophistication and complexity, such as: (a) enzymatic hydrolysis by digestive enzymes; (b) proteolysis of the protein source by enzymes derived from microorganisms or plants; (c) fermentation process using culture with high proteolytic power and specificity. The bioactive potential of the peptides originating from the proteolysis of food proteins can be explored in the integral hydrolysates, produced in special conditions. However, in the current literature there are numerous research works and literature reviews emphasizing the importance of the isolation, purification, characterization, study of mechanisms and impact of these peptides on human health [3][4][5][6][7][8]. Production and Processing of Bioactive Peptides Derived from Food ProteinsA large number of plants and animals have been object of study as source of Bioactive Peptides (BAPs). Several studies were conducted, particularly with milk proteins [9,10], eggs [11,12], and muscle proteins from pigs [13], cattle [14], poultry [15], and fish [16]. BAPs have been obtained from...

show abstract

Section: Antihypertensive Peptidesmentioning

confidence: 99%

mentioning

confidence: 99%

Food Proteins and Bioactive Peptides, Functional Diets

Sgarbieri¹,

Armadas²

2017

FSN

View full text Add to dashboard Cite

show abstract

“…Adicionalmente, verificou-se que as subunidades α e β da hemoglobina de diversos vertebrados apresentam atividade contra bactérias Gram-positivas, Gram-negativas e fungos (Parish et al, 2001) e, nos últimos 10 anos, vários trabalhos têm descrito a atividade antimicrobiana de peptídeos derivados da hidrólise química ou enzimática de hemeproteínas (Froidevaux et al, 2001;Liepke et al, 2003;Mak et al, 2004;Daoud et al, 2005;Nedjar-Arroume et al, 2006;Nedjar-Arroume et al, 2008). Tais peptídeos an-timicrobianos passaram a ser coletivamente denominados hemocidinas (Mak et al, 2000).…”

Section: Hemoglobina Como Fonte De Peptídeos Bioativosunclassified

Untitled

2011

View full text Add to dashboard Cite

RevisãoRevista da Biologia (2010) 6b: 1-6 2 Contato do autor:almenara@usp.br Recebido 19out10 Aceito 10mar11 PublicadoResumo. Nematóides entomopatogênicos são aqueles capazes de matar insetos. Essa propriedade inseticida é decorrente de um tipo bastante peculiar de simbiose estabelecida entre o verme e uma bactéria, sendo este último organismo o responsável pela morte do inseto em si. Além de oferecer dados interessantes para a compreensão biológica dos mecanismos envolvidos na manutenção de uma simbiose, os nematóides entomopatogênicos representam uma ferramenta potencial para controle de insetos-pragas da agricultura e até mesmo de aracnídeos, como carrapatos. Adicionalmente, o estudo de bactérias entomopatogênicas vem permitindo a identificação de diferentes compostos bioativos de origem microbiana. Palavras-chave. Entomopatogênico; nematóide; simbiose; Photorhabdus; Heterorhabditis.Abstract. Entomopathogenic nematodes are those capable of killing insects. This inseticide property is due to a rather peculiar kind of symbiosis established between the worm and bacteria, the latter being the main responsible for the death of the insect. Besides offering interesting data to understand the biological mechanisms involved in symbiosis, the entomopathogenic nematodes represent a potential tool to control insect pests in agriculture and even arachnids like ticks. Additionally, the study of entomopathogenic bacteria is leading to the identification of different bioactive compounds of microbial origin. Keywords Revisão Nematoides Entomopatogênicos (NEPs)Tradicionalmente, organismos parasitas são definidos como aqueles que vivem em associação com outro organismo (hospedeiro) do qual retiram meios para sua sobrevivência e reprodução, normalmente causando danos à saúde da espécie parasitada. É esta a definição encontrada, por exemplo, nos livros didáticos e nos dicionários. Parasitar, portanto, seria a simbiose (associação biológica) na qual um organismo vive junto de outro para tirar proveito, explorar. Por essa razão o termo é empregado não somente em Biologia, mas também pejorativamente, na língua portuguesa, para classificar as pessoas que não trabalham e vivem às custas de outras. Uma idéia bastante difundida é a de que um parasita eficiente seria aquele que causa pouco dano ao hospedeiro, numa forma de "preservar" seu ambiente de vida pelo máximo de tempo possível (Ebert & Herre, 1996). No entanto, estudos mais recentes questionam essa afirmação ao demonstrar uma crescente complexidade dentro deste há-bito de vida (ver a excelente discussão de Maynard-Smith, 1998). Uma questão fundamental no estudo da interação parasita-hospedeiro é a reconstrução da história deste tipo de associação ou, em termos mais biológicos, desta simbiose. É importante reunir dados na tentativa de definir se os parasitas e seus hospedeiros estão coevoluindo, ou seja, sofrendo alterações selecionadas em ambos os organismos durante toda a sua história evolutiva (a mudança de um acarreta mudanças no outro, e vice-versa) ou, alternativamente,...

show abstract

“…7 In our laboratory we further isolated and characterised LVV-haemorphin-7 (β31-40), VVhaemorphin-7 (β32-40), VV-haemorphin-4 (β32-37) 8,9 and two antibacterial peptides corresponding to α1-23 and α107-136 sequences of bovine haemoglobin. 6,10 Isolation of an active peptide from a protein hydrolysate in order to test its biological applications generally involves several chromatographic steps, including pre-fractionation methods such as gel filtration and reversed-phase liquid chromatography.…”

Section: Introductionmentioning

confidence: 99%

Study of a continuous reactor for selective solvent extraction of haemorphins in the course of peptic haemoglobin hydrolysis

Froidevaux

Vercaigne-Marko

Kapel

et al. 2006

J of Chemical Tech & Biotech

Self Cite

View full text Add to dashboard Cite

The continuous hydrolysis of bovine haemoglobin at pH 3 in a triphasic reactor was studied in order to prepare two pure transient and hydrophobic opioid peptides in one step. A continuous stirred-tank reactor was designed to extract continuously and selectively LVV-haemorphin-7 and VV-haemorphin-7 by a butan-2-ol-octan-1-ol mixture in the course of bovine haemoglobin hydrolysis by pepsin immobilised on A568 Duolite resin. The residence time in the aqueous and organic phases was maintained at 1 h. This system allowed a steady state to be achieved for haemorphin concentrations in each phase and the pepsin stability to be maintained. Finally, success was achieved in producing and extracting continuously the two haemorphins in the aqueous/butan-2-ol-octan-1-ol biphasic medium for more than 10 bed volumes of the reactor.

show abstract

New antibacterial peptide derived from bovine hemoglobin

Cited by 116 publications

References 21 publications

Food Proteins and Bioactive Peptides, Functional Diets

Food Proteins and Bioactive Peptides, Functional Diets

Untitled

Study of a continuous reactor for selective solvent extraction of haemorphins in the course of peptic haemoglobin hydrolysis

Contact Info

Product

Resources

About