Purification and Characterization of Heparin from the Italian ClamCallistachione

Luppi, Elisa; Cesaretti, Marina; Volpi, Nicola

doi:10.1021/bm049196b

Cited by 44 publications

(36 citation statements)

References 24 publications

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“…They have been found in many types of organisms from sponges [43,44], to algae [45,46], to sea cucumbers [47,48], fish [49] and clams [50]. It should be noted that all these marine natural products are sulfates.…”

Section: Marine Derived Protease Inhibitorsmentioning

confidence: 99%

“…Ritonavir inhibits HIV replication in the nM range (EC 50 30 nM, EC 90 130 nM) but does not cause cell death of uninfected MT4 cells (IC 50 > 50 M) [69]. Ritonavir contains a hydroxyethyl transition state mimic and has terminal thiazole rings and hydrophobic Phe and Val residues which increase the bioavailability.…”

Section: Aspartic Protease Inhibitors In the Clinicmentioning

confidence: 99%

“…Atazanavir inhibits HIV-1 protease (K i 10 pM) and HIV infected peripheral blood mononuclear cells (IC 50 8-12 nM), and inhibits indinavir-resistant and saquinavir-resistant HIV-1 strains, IC 50 3-100 nM and 4-100 nM, respectively [75,[78][79][80]. A dose of 300mg of atazanavir resulted in plasma levels greater than the EC 50 value for over 24 h [75,[78][79][80].…”

Section: Aspartic Protease Inhibitors In the Clinicmentioning

confidence: 99%

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Proteases: Nature’s Destroyers and the Drugs that Stop Them

Veltri¹

2015

PPIJ

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Proteases are found in all life forms and regulate many cellular pathways. Proteases have been proven as viable drug targets. This paper reviews the mechanism of hydrolysis of the amino acid based aspartic, cysteine, serine and threonine proteases and will also highlight the current anti protease therapeutics in the clinic. the oxygen of the carbonyl drive the cleavage of the peptide bond, which abstracts hydrogen from the general base. Water then releases the second half of the product from the active site residue. The oxyanion hole generated during the transition state is stabilized through hydrogen bonding with amino groups of the backbone. The role of the oxyanion hole is not fully understood [18]. While the chemistry of the mechanism of hydrolysis is similar for serine, aspartic, cysteine and threonine proteases, the amino acids involved in catalysis are what define the various classes. The different classes of proteases are discussed below. Serine ProteasesSerine proteases [19][20][21] use an active site serine to hydrolyze a peptide bond. The other amino acids involved in catalysis vary between the different serine protease groups. The Ser-His-Asp triad can be replaced with Ser-His-Glu, Ser-His-His or Ser-Lys depending on the family of serine protease [20,21]. The serine proteases are categorized by tertiary structures into the super families of the trypsin-like or subtilisin-like [2,19,20]. Examples of the trypsin-like serine proteases, the larger of the super families, are trypsin, chymotrypsin, thrombin, factor IX a, and factor Xa [2,19,20]. Interestingly, some cysteine proteases adopt the trypsin-like structure [22]. Examples of the subtilisin-like serine proteases are proteinase K and thermitase [2,19,20]. Proteases: Nature's Destroyers and the Drugs that Stop Them 3/11Copyright: ©2015 Veltri Citation: Veltri CA (2015) Proteases: Nature's Destroyers and the Drugs that Stop Them. Pharm Pharmacol Int J 2(6): 00044. DOI: 10.15406/ ppij.2015.02.00044Along with tertiary structure, serine proteases are designed against the nature of the P 1 residue recognized by the protease types. The trypsin-like proteases cleave positively charged residues (Lys or Arg are preferred at P 1 ), elastase-like proteases prefer small hydrophobic residues (Ala or Val are preferred at P 1 ) while chymotrypsin-like proteases prefer large hydrophobic residues (Phe, Tyr, or Leu) [2,19,20]. Aspartic ProteasesAspartic proteases [19,[23][24][25][26] use two aspartic acid residues to hydrolyze a peptide bond. These proteases are categorized into the super families of pepsin-like or viral retropepsin-like due to the tertiary structure [23,24,26,27]. The pepsin-like include pepsin, cathepsin D and chymosin [23,27]. The viral retropepsinlike include the retro pepsins of the immune viruses HIV, FIV and SIV [24,26].Aspartic proteases are unique in the fact they do not have a His residue in their active site. The general acid-base mechanism proposed for peptide hydrolysis involves two Asp residues and uses water to attack the targe...

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Section: Marine Derived Protease Inhibitorsmentioning

confidence: 99%

Section: Aspartic Protease Inhibitors In the Clinicmentioning

confidence: 99%

Section: Aspartic Protease Inhibitors In the Clinicmentioning

confidence: 99%

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Proteases: Nature’s Destroyers and the Drugs that Stop Them

Veltri¹

2015

PPIJ

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“…Linear PAGE in a barbital buffer (Fig. 8) has also been utilized for the determination of the molecular mass of Hep samples extracted and purified from several molluscs [71,72]. Actually, PAGE is a powerful technique for a rapid sequencing of HS and Hep saccharides [73] and for the characterization and quantitation of HA and CS/DS saccharides [74].…”

Section: Electrophoresis On Polyacrylamide Gel (Page)mentioning

confidence: 99%

Electrophoretic approaches to the analysis of complex polysaccharides

Volpi

Maccari

2006

Journal of Chromatography B

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“…A few well-known examples include hyaluronic acid (HA), chondroitin sulfate (CS)/dermatan sulfate (DS), and heparin (HP)/heparan sulfate. The presence of GAGs in some mollusks has now been well established but with variations in the relative amounts, molecular mass and sulfation (Cássaro & Dietrich, 1977;Chavante et al, 2000;Dietrich et al, 1985;Jordan & Marcum, 1986;Li et al, 2011;Luppi, Cesaretti, & Volpi, 2005;Nicola & Francesca, 2005, 2007, 2009Pejler et al, 1987;Volpi & Maccari, 2008). In addition, non-glycosaminoglycan polysaccharides with uronic acids are also identified (Wang, Jun, & Li, 2015).…”

Section: Introductionmentioning

confidence: 99%