L-Phenylalanine b-naphthylamide
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L-Phenylalanine b-naphthylamide

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A substrate for aminopeptidase M (microsomal alanyl aminopeptidase).

Category
L-Amino Acids
Catalog number
BAT-004020
CAS number
740-57-8
Molecular Formula
C19H18N2O
Molecular Weight
290.32
L-Phenylalanine b-naphthylamide
IUPAC Name
(2S)-2-amino-N-naphthalen-2-yl-3-phenylpropanamide
Synonyms
L-Phe-bNA; L-Phenylalanine-B-Naphthylamide; N-L-Phenylalanyl-2-naphthylamin; L-Phenylalanine-Naphthylamide; L-Phenylalanin-[2]naphthylamid
Appearance
White powder
Purity
≥ 99% (TLC)
Density
1.220±0.06 g/cm3
Melting Point
126-130 °C
Boiling Point
550.4±43.0 °C
Storage
Store at 2-8 °C
InChI
InChI=1S/C19H18N2O/c20-18(12-14-6-2-1-3-7-14)19(22)21-17-11-10-15-8-4-5-9-16(15)13-17/h1-11,13,18H,12,20H2,(H,21,22)/t18-/m0/s1
InChI Key
QUOLUWPVABJBKU-SFHVURJKSA-N
Canonical SMILES
C1=CC=C(C=C1)CC(C(=O)NC2=CC3=CC=CC=C3C=C2)N
1. Effects of proteinase inhibitors on fertilization in sea lamprey (Petromyzon marinus)
Konrad Dabrowski, Jan Glogowski, Andrzej Ciereszko Comp Biochem Physiol B Biochem Mol Biol. 2004 Oct;139(2):157-62. doi: 10.1016/j.cbpc.2004.06.010.
A search for alternative sterilants in parasitic fish encouraged us to explore the usefulness of proteinase inhibitors for this purpose. Fertilization in sea lamprey species (Petromyzon marinus L.) was inhibited by chymotrypsin and trypsin inhibitors 4'-acetamidophenyl 4-guanidinobenzoate (AGB), chymostatin, tosyl-L-lysine chloromethyl ketone (TLCK), and N-tosyl-L-phenylalanine chloromethyl ketone (TPCK) when these substances were added into a fertilization medium at the time of fertilization. Preincubation of eggs before fertilization with 100 microM TPCK, but not TLCK, resulted in inhibition of fertilization. Conversely, preincubation of spermatozoa with TLCK, but not TPCK, produced inhibition of fertilization. These data suggest the involvement of the chymotrypsin-like activity of eggs and trypsin-like activity of spermatozoa in fertilization. However, enzymes present in sperm suspensions were able to hydrolyze a chymotrypsin substrate N-glutaryl-L-phenylalanine-p-nitroanilide (GPNA) but not trypsin substrate N-alpha-benzoyl-DL-arginine-p-nitroanilide (BAPNA). The nature of this activity can be characterized as serine protease and our results indicate the involvement of serine proteinases in the fertilization of sea lamprey.
2. Coagulation protein function: the influence of acetaldehyde-modified heparin on thrombin activity
A S Brecher, Q Fu J Investig Med. 1999 Jan;47(1):76-80.
Background: The affect of acetaldehyde-treated heparin on thrombin activity has been investigated using factor II-deficient human plasma. Methods: It was observed that 0.021 units of heparin exerts a marked inhibition of thrombin activity (1.03 units) as measured by clotting times, prolonging the clotting times from 9.6 +/- 0.1 seconds to 24.8 +/- 0.1 seconds. However, when the heparin is preincubated with 447 mmol/L acetaldehyde at RT for 30 minutes prior to mixing with thrombin, a clotting time in excess of 200 seconds is observed. Clotting times remain elevated with heparin-acetaldehyde mixtures of 89.4, 17.9, 3.6, and 0.72 mmol/L acetaldehyde, with corresponding clotting times of > 200, 156.0 +/- 2.1, 81.6 +/- 1.0, 38.8 +/- 0.6 seconds, respectively. At 140 mumol/L acetaldehyde-heparin mixtures, the clotting time was 17.0 +/- 2.0 seconds. Results: These data support the hypothesis from this laboratory that acetaldehyde-modified heparin enhances coagulation time. They further indicate that thrombin is targeted by the acetaldehyde-treated heparin. Heparin-acetaldehyde mixtures also reacted with plasma prior to the addition of thrombin to modestly prolong coagulation time. Similarly, but more effectively, thrombin/heparin mixtures increased the clotting time of acetaldehyde-exposed plasma. These data further suggest the possibility that reactions of acetaldehyde and heparin are not restricted to those with thrombin, and that they may extend to other blood factors/proteins. Conclusions: The amount of heparin (0.021 units) required to substantially affect clotting time of thrombin (1.03 units) is substantially lower than that required to prolong clotting of 0.1 mL of whole plasma (0.36 units), by an order of magnitude. It is inferred that heparin may interact with numerous cationic proteins or proteins with cationic domains in blood plasma, among them being the clotting factors.
3. The effect of glycosaminoglycans with acetaldehyde on the activation of prothrombin
Arthur S Brecher, Mohammed T Adamu Can J Physiol Pharmacol. 2005 May;83(5):431-8. doi: 10.1139/y05-017.
Heparin17-19k, (25, 50, and 100 ng), heparin6k (50 and 100 ng), heparin3k (50, 100, and 200 microg), chondroitin sulfates B (dermatan sulfate) (0.25, 0.5, and 1.0 microg), C (1 and 10 microg), and A (1 and 10 microg) each prolong the activated partial thromboplastin time (APTT) when preincubated with prothrombin to a greater extent than when preincubated with Factor II-deficient plasma prior to their mixing and subsequent additions of APTT reagent and Ca2+. In all cases statistical significance (p < or = 0.05) was observed except with the 2 lower levels of heparin3k. These results suggest that the glycosaminoglycans (GAGs) may exert a direct effect upon prothrombin (FII) in their anticoagulant activity. Pre mix tures of [(FII/25 ng H17-19k) + 447 mmol acetaldehyde (AcH)/L] as well as [(AcH/H) + FII] and [(FII/AcH) + H] each exert a synergistic anticoagulant effect upon APTT. At low AcH concentrations (44.7 mmol/L), neither a synergistic nor an additive effect is seen. H6k and H3k, on premixing with 447 mmol AcH/L, exhibit an additive effect on APTT prolongation but no synergism. Similarly, premixtures of CSB/447 mmol AcH/L/FII show a greater anticoagulant effect than do [(CSB/AcH) + FII] or [(FII/AcH) + CSB] premixtures. CSC-AcH and CSA-AcH patterns are analogous to those of CSB (DS). These data suggest the possibility that AcH, the primary product of ethanol metabolism, may serve as a crosslinking adduct with proteins, in this case, prothrombin, as well as GAGs. Thus ternary complexes between the zymogen form of coagulation factors, GAGs, and AcH are possible, further influencing coagulopathy.
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