Antimicrobial Activity of a Bovine Hemoglobin Fragment in the Tick Boophilus microplus

Fogaça, Andréa Cristina; Silva, Pedro I. da; Miranda, Maria Terêsa Machini de; Bianchi, A.G. de; Miranda, Antônio; Ribolla, Paulo Eduardo Martins; Daffre, Sirlei

doi:10.1074/jbc.274.36.25330

Cited by 179 publications

(148 citation statements)

References 28 publications

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“…Antimicrobial proteins and peptides have been obtained from a variety of sources such as aquatic organisms like shrimp (Cuthbertson et al, 2002), sole (Oren and Shai, 1996), flounder (Cole et al, 1997), and anchovy (Tang et al, 2015), plants (Capriotti et al, 2015), blood (Fogaca et al, 1999), milk (McCann et al, 2006), and egg (Mine et al, 2004), to name a few. One of the latest investigations to derive antimicrobial peptides from natural sources was the work performed by Capriotti et al (2015).…”

Section: Antimicrobial Effectmentioning

confidence: 99%

Peptides: Production, bioactivity, functionality, and applications

Hajfathalian

Ghelichi

Moreno

et al. 2017

Critical Reviews in Food Science and Nutrition

138

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Production of peptides with various effects from proteins of different sources continues to receive academic attention. Researchers of different disciplines are putting increasing efforts to produce bioactive and functional peptides from different sources such as plants, animals, and food industry by-products. The aim of this review is to introduce production methods of hydrolysates and peptides and provide a comprehensive overview of their bioactivity in terms of their effects on immune, cardiovascular, nervous, and gastrointestinal systems. Moreover, functional and antioxidant properties of hydrolysates and isolated peptides are reviewed. Finally, industrial and commercial applications of bioactive peptides including their use in nutrition and production of pharmaceuticals and nutraceuticals are discussed.

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Section: Antimicrobial Effectmentioning

confidence: 99%

Peptides: Production, bioactivity, functionality, and applications

Hajfathalian

Ghelichi

Moreno

et al. 2017

Critical Reviews in Food Science and Nutrition

138

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“…Fogaca et al, [44] identified and sequenced the first antimicrobial peptides from bovine Hemoglobin (Hb). The sequence of amino acids was identified by mass spectrometry: Phe-Leu-Ser-Phe-Pro-ThrThr-Lys-Thr-Tyr-Phe-Pro-His-Phe-Asp-Leu-Ser-His-Gly-Ser-AlaGly-Val-Lys-Gly-Hys-Gly-Ala-Lys (MM 3,205.7Da) corresponding to the (f: 33-61) of α-hemoglobin.…”

Section: Antimicrobial Activitymentioning

confidence: 99%

“…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%

“…A JF2 peptide containing 26 amino acid residues was isolated from Japanese flounder (Paralichthys olivaceus) which showed antimicrobial activity against Gram (-) Escherichia coli and Gram (+) Streptooccus aureus and Lacrococcus garvieae, but had no effect on the Gram (-) bacteria Edwardsiella tarda [43]. Expression of the JF2 peptide was observed in the liver, heart, kidneys, spleen, and stomach of the flounder.Fogaca et al, [44] identified and sequenced the first antimicrobial peptides from bovine Hemoglobin (Hb). The sequence of amino acids was identified by mass spectrometry: Phe-Leu-Ser-Phe-Pro-ThrThr-Lys-Thr-Tyr-Phe-Pro-His-Phe-Asp-Leu-Ser-His-Gly-Ser-AlaGly-Val-Lys-Gly-Hys-Gly-Ala-Lys (MM 3,205.7Da) corresponding to the (f: 33-61) of α-hemoglobin.…”

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confidence: 99%

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Food Proteins and Bioactive Peptides, Functional Diets

Sgarbieri¹,

Armadas²

2017

FSN

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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...

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“…Como realizam digestão intracelular, os patógenos não sofrem o ataque de enzimas digestivas no intestino dos carrapatos. Porém, já foi demonstrada a presença de peptídeos antimicrobianos (PAM) resultantes da digestão da hemoglobina do hospedeiro no intestino (Belmonte et al, 2012;Fogaça et al, 1999;Nakajima et al, 2002;Sonenshine et al, 2005). Além dos fragmentos de hemoglobina, PAM como defensinas e lisozimas também foram identificados nos intestinos de algumas espécies de carrapatos (Anderson, Magnarelli, 2008;Kopácek et al, 1999;Nakajima et al, 2002;Sonenshine et al, 2002).…”

Section: A Aquisição E a Transmissão De Riquétsias Por Carrapatosunclassified

Efeitos da infecção por Rickettsia rickettsii sobre o perfil de expressão gênica do carrapato vetor Amblyomma cajennense.

Martins¹

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Antimicrobial Activity of a Bovine Hemoglobin Fragment in the Tick Boophilus microplus

Cited by 179 publications

References 28 publications

Peptides: Production, bioactivity, functionality, and applications

Peptides: Production, bioactivity, functionality, and applications

Food Proteins and Bioactive Peptides, Functional Diets

Efeitos da infecção por Rickettsia rickettsii sobre o perfil de expressão gênica do carrapato vetor Amblyomma cajennense.

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