4-Phenylbutylamine
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| Formula | C10H15N |
| Molar mass | 149.237 g·mol−1 |
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| H314, H315, H319, H335 | |
| P260, P264, P264+P265, P271, P280, P301+P330+P331, P302+P352, P302+P361+P354, P304+P340, P305+P351+P338, P305+P354+P338, P316, P319, P321, P332+P317, P337+P317, P362+P364, P363, P403+P233, P405, P501 | |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
Infobox references
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4-Phenylbutylamine, also known as benzenebutanamine, or 4-PBA, is a phenylalkylamine or phenylbutylamine, consisting of a benzene ring in which one of the hydrogen atoms is substituted by a 4-aminobutyl group. It is a primary amine and a member of the benzene class of organic compounds. It it penetrates lipid bilayers in the cubic liquid-crystalline phase[2] , the 4-phenylbutylamine molecule exists in the form of four stable rotamers.[3]
serine protease inhibitor, It has been used in research as a test inhibitor to study the function of the enzyme trypsin; it is capable of mimicking the side chain of the amino acid lysine or arginine, which allows it to bind to the active site of the enzyme trypsin.[1][4][5]
Modification of hen egg-white lysozyme with 4-phenylbutylamine using EDC creates derivatives with 0.6-0.7 modified residues and about 60 percent activity. Kinetic data shows that this modified lysozyme increases the kcat of SucGly2Phe-4-nitroanilide hydrolysis by α-chymotrypsin by 20 times, without changing the Km. The apparent dissociation constant (Kd) for the lysozyme-chymotrypsin complex is 0.03 mM and does not depend on substrate concentration. This effect is specific to α and δ-chymotrypsins; other serine proteases or similar derivatives of ribonuclease and α-lactalbumin do not show this enhancement. Because chitin oligomers like GlcNAc2 and GlcNAc3 partially block the activation, the 4-phenylbutylamine group is likely located near the lysozyme binding site[6][7].
References
- ^ a b PubChem. "Benzenebutanamine". pubchem.ncbi.nlm.nih.gov. Retrieved 2026-02-02.
- ^ Engström S, Nordén TP, Nyquist H (August 1999). "Cubic phases for studies of drug partition into lipid bilayers". European Journal of Pharmaceutical Sciences : Official Journal of the European Federation for Pharmaceutical Sciences. 8 (4): 243–54. doi:10.1016/s0928-0987(99)00012-3. PMID 10425374.
- ^ "Theoretical and experimental vibrational spectroscopy study on rotational isomer of 4-phenylbutylamine".
{{cite web}}: CS1 maint: url-status (link) - ^ Leiros HK, Brandsdal BO, Andersen OA, Os V, Leiros I, Helland R, et al. (April 2004). "Trypsin specificity as elucidated by LIE calculations, X-ray structures, and association constant measurements". Protein Science. 13 (4): 1056–1070. doi:10.1110/ps.03498604. PMC 2280040. PMID 15044735.
- ^ "4-Phenylbutylamine". go.drugbank.com. Retrieved 2026-02-02.
- ^ Shechter Y, Gertler A (1978-11-10). "Enhancement of α-chymotrypsin-catalyzed hydrolysis of specific p-nitroanilide substrates by 4-phenylbutylamine derivative of hen egg-white lysozyme". Biochimica et Biophysica Acta (BBA) - Enzymology. 527 (1): 42–55. doi:10.1016/0005-2744(78)90254-1. ISSN 0005-2744.
- ^ Shechter Y, Gertler A (1978-11-10). "Enhancement of alpha-chymotrypsin-catalyzed hydrolysis of specific p-nitroanilide substrates by 4-phenylbutylamine derivative of hen egg-white lysozyme". Biochimica Et Biophysica Acta. 527 (1): 42–55. doi:10.1016/0005-2744(78)90254-1. ISSN 0006-3002. PMID 718965.