Capsazepine blocks the painful sensation of heat caused by capsaicin (the active ingredient of
chilli pepper) which activates the
TRPV1 ion channel. Capsazepine is therefore considered to be a TRPV1
antagonist. The TRPV1 channel functions as a pain and temperature sensor in
mammalians. Capsazepine blocks the activation of TRPV1 channels by other chemicals, but not by other painful stimuli such as heat. Depending on the pharmacological assay, the
IC50 is in the
nanomolar to low
micromolar range. In addition to its effects on TRPV1 channels, it was also shown to activate the noxious chemical sensor
TRPA1 channel,[2] inhibit the cold activated
TRPM8 channel,[3]voltage-activated calcium channels[4] and
nicotinic acetylcholine receptors.[5] It mainly serves as a tool to study the TRPV1 ion channel.[6]
Development
Capsazepine was discovered by a research group working for
Novartis.[1] Its synthesis and chemical properties were published in 1994. It was found by modification of the chemical backbone of capsaicin.[7]
Use in biotechnology
By incorporation of an
azobenzene unit, a
photoswitchable version of capsazepine (AC4) was developed in 2013 that allows for optical control of
TRPV1 channels with light.[8][9]
^Walpole CS, Bevan S, Bovermann G, Boelsterli JJ, Breckenridge R, Davies JW, Hughes GA, James I, Oberer L, Winter J (June 1994). "The discovery of capsazepine, the first competitive antagonist of the sensory neuron excitants capsaicin and resiniferatoxin". Journal of Medicinal Chemistry. 37 (13): 1942–54.
doi:
10.1021/jm00039a006.
PMID8027976.
^Stein M, Breit A, Fehrentz T, Gudermann T, Trauner D (September 2013). "Optical control of TRPV1 channels". Angewandte Chemie. 52 (37): 9845–8.
doi:
10.1002/anie.201302530.
PMID23873837.
Capsazepine blocks the painful sensation of heat caused by capsaicin (the active ingredient of
chilli pepper) which activates the
TRPV1 ion channel. Capsazepine is therefore considered to be a TRPV1
antagonist. The TRPV1 channel functions as a pain and temperature sensor in
mammalians. Capsazepine blocks the activation of TRPV1 channels by other chemicals, but not by other painful stimuli such as heat. Depending on the pharmacological assay, the
IC50 is in the
nanomolar to low
micromolar range. In addition to its effects on TRPV1 channels, it was also shown to activate the noxious chemical sensor
TRPA1 channel,[2] inhibit the cold activated
TRPM8 channel,[3]voltage-activated calcium channels[4] and
nicotinic acetylcholine receptors.[5] It mainly serves as a tool to study the TRPV1 ion channel.[6]
Development
Capsazepine was discovered by a research group working for
Novartis.[1] Its synthesis and chemical properties were published in 1994. It was found by modification of the chemical backbone of capsaicin.[7]
Use in biotechnology
By incorporation of an
azobenzene unit, a
photoswitchable version of capsazepine (AC4) was developed in 2013 that allows for optical control of
TRPV1 channels with light.[8][9]
^Walpole CS, Bevan S, Bovermann G, Boelsterli JJ, Breckenridge R, Davies JW, Hughes GA, James I, Oberer L, Winter J (June 1994). "The discovery of capsazepine, the first competitive antagonist of the sensory neuron excitants capsaicin and resiniferatoxin". Journal of Medicinal Chemistry. 37 (13): 1942–54.
doi:
10.1021/jm00039a006.
PMID8027976.
^Stein M, Breit A, Fehrentz T, Gudermann T, Trauner D (September 2013). "Optical control of TRPV1 channels". Angewandte Chemie. 52 (37): 9845–8.
doi:
10.1002/anie.201302530.
PMID23873837.