Bidesmosidic Triterpenoidal Saponins from the Roots of<i>Symphytum officinale</i>

Mohammad, Faryal Vali; Noorwala, Mushtaq; Ahmad, Viqar Uddin; Şener, Bilge

doi:10.1055/s-2006-958017

Cited by 14 publications

(7 citation statements)

References 2 publications

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“…They show little to no presence of hydrophobic residues and a higher random coil structure. These peptides are known to possess antimicrobial activity against gram-positive and gram-negative bacteria with membrane-disruptive and non-membrane-disruptive mechanisms (Mohammad et al, 1995;Powers and Hancock, 2003).…”

Section: Antimicrobial Effect Of Porcine Blood Protein Hydrolysatesmentioning

confidence: 99%

Hydrolysis Conditions of Porcine Blood Proteins and Antimicrobial Effects of Their Hydrolysates

Jin¹,

Choi²,

Yim³

2020

Food Sci Anim Resour

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In the present study, we determined the degree of hydrolysis (DH) of porcine blood plasma proteins, albumin, and globulin hydrolyzed by six proteases (alcalase, neutrase, flavourzyme, protamex, trypsin, and papain) for various reaction times. Moreover, antimicrobial activities of hydrolysates against five pathogenic microorganisms (Bacillus cereus, Staphylococcus aureus, Salmonella Typhimurium, Escherichia coli, and Shigella flexneri) were investigated. Alcalase, trypsin, and papain hydrolysates of the three porcine blood proteins showed higher DH values than hydrolysates produced by the other three proteases. DH of the three porcine blood proteins hydrolyzed by the six proteases failed to increase after 2 h of hydrolysis. In antimicrobial tests, hydrolysates (hydrolysis time of 2 h) showed antibacterial activity only against B. cereus. Albumin hydrolysates showed higher antimicrobial activity than globulin and plasma hydrolysates. Albumin hydrolysates obtained with flavourzyme, protamex, and trypsin showed higher antimicrobial activity than those obtained with the other three proteases.

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Section: Antimicrobial Effect Of Porcine Blood Protein Hydrolysatesmentioning

confidence: 99%

Hydrolysis Conditions of Porcine Blood Proteins and Antimicrobial Effects of Their Hydrolysates

Jin¹,

Choi²,

Yim³

2020

Food Sci Anim Resour

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“…A common feature shared among the cationic AMPs is their ability to fold into amphipathic conformations, often induced by interaction with membranes or membrane mimics. Alongside their direct antimicrobial activities against Gram-positive and Gramnegative bacteria, these peptides play additional roles as antibiotics against fungi [7] and protozoa [8] with micromolar or submicromolar minimal inhibitory concentrations (MIC) [6].…”

mentioning

confidence: 99%

Antimicrobial peptides: an overview of a promising class of therapeutics

Giuliani¹,

Pirri²,

Nicoletto³

2007

Open Life Sciences

465

459

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Antibiotic resistance is increasing at a rate that far exceeds the pace of new development of drugs. Antimicrobial peptides, both synthetic and from natural sources, have raised interest as pathogens become resistant against conventional antibiotics. Indeed, one of the major strengths of this class of molecules is their ability to kill multidrug-resistant bacteria. Antimicrobial peptides are relatively small (6 to 100 aminoacids), amphipathic molecules of variable length, sequence and structure with activity against a wide range of microorganisms including bacteria, protozoa, yeast, fungi, viruses and even tumor cells. They usually act through relatively non-specific mechanisms resulting in membranolytic activity but they can also stimulate the innate immune response. Several peptides have already entered pre-clinical and clinical trials for the treatment of catheter site infections, cystic fibrosis, acne, wound healing and patients undergoing stem cell transplantation. We review the advantages of these molecules in clinical applications, their disadvantages including their low in vivo stability, high costs of production and the strategies for their discovery and optimization.

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“…[5] AMPs from different sources possess a broad range of activity, showing activities against bacteria, fungi, viruses, and protozoa. [6][7][8] Additional emerging uses for cationic AMPs include use in laboratory transfection techniques and also as antisepsis agents, due to their ability to bind lipopolysaccharide (LPS). [9,10] Rationally designed short cationic AMPs may be able to supplement the currently available spectrum of therapeutic antibiotics by providing increased pathogen selectivity, unique mechanisms of action, and novelty in molecular structure by chemical modification.…”

Section: Introductionmentioning

confidence: 99%

Hydrocarbon‐stapled lipopeptides exhibit selective antimicrobial activity

et al. 2017

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Antimicrobial peptides (AMPs) occur widely in nature and have been studied for their therapeutic potential. AMPs are of interest due to the large number of possible chemical structural combinations using natural and unnatural amino acids, with varying effects on their biological activities. Using physicochemical properties from known naturally occurring amphipathic cationic AMPs, several hydrocarbon-stapled lipopeptides (HSLPs) were designed, synthesized, and tested for antimicrobial properties. Peptides were chemically modified by N-terminal acylation, C-terminal amidation, and some were hydrocarbon stapled by intramolecular olefin metathesis. The effects of peptide length, amphipathic character, and stapling on antimicrobial activity were tested against Escherichia coli, three species of Gram-positive bacteria (Staphylococcus aureus, Bacillus megaterium, and Enterococcus faecalis), and two strains of Candida albicans. Peptides were shown to disrupt liposomes of different phospholipid composition, as measured by leakage of a fluorescent compound from vesicles. Peptides with (S)-2-(4'-pentenyl)-alanine substituted for l-alanine in a reference peptide showed a marked increase in antimicrobial activity, hemolysis, and membrane disruption. Stapled peptides exhibited slightly higher antimicrobial potency; those with greatest hydrophobic character showed the greatest hemolysis and liposome leakage, but lower antimicrobial activity. The results support a model of HSLPs as membrane-disruptive AMPs with potent antimicrobial activity and relatively low hemolytic potential at biologically active peptide concentrations.

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Bidesmosidic Triterpenoidal Saponins from the Roots ofSymphytum officinale

Cited by 14 publications

References 2 publications

Hydrolysis Conditions of Porcine Blood Proteins and Antimicrobial Effects of Their Hydrolysates

Hydrolysis Conditions of Porcine Blood Proteins and Antimicrobial Effects of Their Hydrolysates

Antimicrobial peptides: an overview of a promising class of therapeutics

Hydrocarbon‐stapled lipopeptides exhibit selective antimicrobial activity

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