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Shuo Huang - One of the best experts on this subject based on the ideXlab platform.
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A single molecule observAtion of dichloroAurAte i binding to An engineered mycobActerium smegmAtis Porin A mspA nAnopore
Analytical Chemistry, 2021Co-Authors: Jiao Cao, Wendong Jia, Jinyue Zhang, Shuanghong Yan, Yuqin Wang, Panke Zhang, Hongyuan Chen, Shanyu Zhang, Sha Wang, Shuo HuangAbstract:Gold(I) compounds Are known to bind sulfur-contAining proteins, forming the bAsis in the design of gold(I)-bAsed drugs. However, the intrinsic moleculAr mechAnism of the chemicAl reAction is eAsily hidden when monitored in ensemble. We hAve previously demonstrAted thAt MycobActerium smegmAtis Porin A (MspA) cAn be engineered (MspA-M) to contAin A speciAlized nAnoreActor to probe chemicAl reActions involving tetrAchloroAurAte(III). Here, we provide further investigAtions of coordinAtion interActions between dichloroAurAte(I) And MspA-M. Gold compounds of different coordinAtion geometry And vAlence stAtes Are As well probed And evAluAted, demonstrAting the generAlity of MspA-M. With single-molecule evidence, MspA-M demonstrAtes A preference for dichloroAurAte(I) thAn tetrAchloroAurAte(III), An observAtion in A single molecule thAt hAs never been reported. By counting the mAximum number of simultAneous ion bindings, the nArrowly confined pore restriction Also efficiently distinguishes dichloroAurAte(I) And tetrAchloroAurAte(III) According to their differences in geometry or size. The Above demonstrAtion complemented A previous study by demonstrAting other possible gold-bAsed single-molecule chemicAl reActions observAble by MspA. These observAtions bring insights in the understAnding of gold-bAsed coordinAtion chemistry in A nAnoscAle.
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single molecule observAtion of hArd soft Acid bAse hsAb interAction in engineered mycobActerium smegmAtis Porin A mspA nAnopores
Chemical Science, 2020Co-Authors: Sha Wang, Jiao Cao, Wendong Jia, Shuanghong Yan, Yuqin Wang, Panke Zhang, Hongyuan Chen, Weiming Guo, Shuo HuangAbstract:In the formAtion of coordinAtion interActions between metAl ions And Amino Acids in nAturAl metAlloproteins, the bound metAl ion is criticAl either for the stAbilizAtion of the protein structure or As An enzyme co-fActor. Though extremely smAll in size, metAl ions, when bound to the restricted environment of An engineered biologicAl nAnopore, result in detectAble perturbAtions during single chAnnel recordings. All reported work of this kind wAs performed with engineered α-hemolysin nAnopores And the observed events AppeAr to be extremely smAll in Amplitude (∼1–3 pA). We speculAte thAt the cylindricAl pore restriction of α-hemolysin mAy not be optimAl for probing extremely smAll AnAlytes. MycobActerium smegmAtis Porin A (MspA), A conicAl shAped nAnopore, wAs engineered to interAct with CA2+, Mn2+, Co2+, Ni2+, Zn2+, Pb2+ And Cd2+ And A systemAticAlly lArger event Amplitude (up to 10 pA) wAs observed. The meAsured rAte constAnt suggests thAt the coordinAtion of A single ion with An Amino Acid follows hArd–soft-Acid–bAse theory, which hAs never been systemAticAlly vAlidAted in the cAse of A single molecule. By Adjusting the meAsurement pH from 6.8 to 8.0, the durAtion of A single ion binding event could be modified with A ∼46-fold time extension. The phenomenA reported suggest MspA to be A superior engineering templAte for probing A vAriety of extremely smAll AnAlytes, such As monAtomic And polyAtomic ions, smAll molecules or chemicAl intermediAtes, And the principle of hArd–soft-Acid–bAse interAction mAy be instructive in the pore design.
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giAnt single molecule chemistry events observed from A tetrAchloroAurAte iii embedded mycobActerium smegmAtis Porin A nAnopore
Nature Communications, 2019Co-Authors: Jiao Cao, Wendong Jia, Jinyue Zhang, Shuanghong Yan, Yuqin Wang, Panke Zhang, Hongyuan Chen, Shuo HuangAbstract:BiologicAl nAnopores Are cApAble of resolving smAll AnAlytes down to A monoAtomic ion. In this reseArch, tetrAchloroAurAte(III), A polyAtomic ion, is discovered to bind to the methionine residue (M113) of A wild-type α-hemolysin by reversible Au(III)-thioether coordinAtion. However, the cylindricAl pore geometry of α-hemolysin generAtes shAllow ionic binding events (~5–6 pA) And mAy hAve introduced other undesired interActions. Inspired by nAnopore sequencing, A MycobActerium smegmAtis Porin A (MspA) nAnopore, which possesses A conicAl pore geometry, is mutAted to bind tetrAchloroAurAte(III). Subsequently, further Amplified blockAge events (up to ~55 pA) Are observed, which report the lArgest single ion binding event from A nAnopore meAsurement. By tAking the embedded Au(III) As An Atomic bridge, the MspA nAnopore is enAbled to discriminAte between different biothiols from single molecule reAdouts. These phenomenA suggest thAt MspA is AdvAntAgeous for single molecule chemistry investigAtions And hAs ApplicAtions As A hybrid biologicAl nAnopore with Atomic AdAptors. Engineered biologicAl nAnopores enAble observAtion of single molecule chemistry events; however A cylindricAl pore geometry cAn hAve undesired effects. The Authors report A conicAl biologicAl pore which wAs embedded with tetrAchloroAurAte(III) to Allow for discriminAtion between different biothiols.
Jiao Cao - One of the best experts on this subject based on the ideXlab platform.
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A single molecule observAtion of dichloroAurAte i binding to An engineered mycobActerium smegmAtis Porin A mspA nAnopore
Analytical Chemistry, 2021Co-Authors: Jiao Cao, Wendong Jia, Jinyue Zhang, Shuanghong Yan, Yuqin Wang, Panke Zhang, Hongyuan Chen, Shanyu Zhang, Sha Wang, Shuo HuangAbstract:Gold(I) compounds Are known to bind sulfur-contAining proteins, forming the bAsis in the design of gold(I)-bAsed drugs. However, the intrinsic moleculAr mechAnism of the chemicAl reAction is eAsily hidden when monitored in ensemble. We hAve previously demonstrAted thAt MycobActerium smegmAtis Porin A (MspA) cAn be engineered (MspA-M) to contAin A speciAlized nAnoreActor to probe chemicAl reActions involving tetrAchloroAurAte(III). Here, we provide further investigAtions of coordinAtion interActions between dichloroAurAte(I) And MspA-M. Gold compounds of different coordinAtion geometry And vAlence stAtes Are As well probed And evAluAted, demonstrAting the generAlity of MspA-M. With single-molecule evidence, MspA-M demonstrAtes A preference for dichloroAurAte(I) thAn tetrAchloroAurAte(III), An observAtion in A single molecule thAt hAs never been reported. By counting the mAximum number of simultAneous ion bindings, the nArrowly confined pore restriction Also efficiently distinguishes dichloroAurAte(I) And tetrAchloroAurAte(III) According to their differences in geometry or size. The Above demonstrAtion complemented A previous study by demonstrAting other possible gold-bAsed single-molecule chemicAl reActions observAble by MspA. These observAtions bring insights in the understAnding of gold-bAsed coordinAtion chemistry in A nAnoscAle.
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single molecule observAtion of hArd soft Acid bAse hsAb interAction in engineered mycobActerium smegmAtis Porin A mspA nAnopores
Chemical Science, 2020Co-Authors: Sha Wang, Jiao Cao, Wendong Jia, Shuanghong Yan, Yuqin Wang, Panke Zhang, Hongyuan Chen, Weiming Guo, Shuo HuangAbstract:In the formAtion of coordinAtion interActions between metAl ions And Amino Acids in nAturAl metAlloproteins, the bound metAl ion is criticAl either for the stAbilizAtion of the protein structure or As An enzyme co-fActor. Though extremely smAll in size, metAl ions, when bound to the restricted environment of An engineered biologicAl nAnopore, result in detectAble perturbAtions during single chAnnel recordings. All reported work of this kind wAs performed with engineered α-hemolysin nAnopores And the observed events AppeAr to be extremely smAll in Amplitude (∼1–3 pA). We speculAte thAt the cylindricAl pore restriction of α-hemolysin mAy not be optimAl for probing extremely smAll AnAlytes. MycobActerium smegmAtis Porin A (MspA), A conicAl shAped nAnopore, wAs engineered to interAct with CA2+, Mn2+, Co2+, Ni2+, Zn2+, Pb2+ And Cd2+ And A systemAticAlly lArger event Amplitude (up to 10 pA) wAs observed. The meAsured rAte constAnt suggests thAt the coordinAtion of A single ion with An Amino Acid follows hArd–soft-Acid–bAse theory, which hAs never been systemAticAlly vAlidAted in the cAse of A single molecule. By Adjusting the meAsurement pH from 6.8 to 8.0, the durAtion of A single ion binding event could be modified with A ∼46-fold time extension. The phenomenA reported suggest MspA to be A superior engineering templAte for probing A vAriety of extremely smAll AnAlytes, such As monAtomic And polyAtomic ions, smAll molecules or chemicAl intermediAtes, And the principle of hArd–soft-Acid–bAse interAction mAy be instructive in the pore design.
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giAnt single molecule chemistry events observed from A tetrAchloroAurAte iii embedded mycobActerium smegmAtis Porin A nAnopore
Nature Communications, 2019Co-Authors: Jiao Cao, Wendong Jia, Jinyue Zhang, Shuanghong Yan, Yuqin Wang, Panke Zhang, Hongyuan Chen, Shuo HuangAbstract:BiologicAl nAnopores Are cApAble of resolving smAll AnAlytes down to A monoAtomic ion. In this reseArch, tetrAchloroAurAte(III), A polyAtomic ion, is discovered to bind to the methionine residue (M113) of A wild-type α-hemolysin by reversible Au(III)-thioether coordinAtion. However, the cylindricAl pore geometry of α-hemolysin generAtes shAllow ionic binding events (~5–6 pA) And mAy hAve introduced other undesired interActions. Inspired by nAnopore sequencing, A MycobActerium smegmAtis Porin A (MspA) nAnopore, which possesses A conicAl pore geometry, is mutAted to bind tetrAchloroAurAte(III). Subsequently, further Amplified blockAge events (up to ~55 pA) Are observed, which report the lArgest single ion binding event from A nAnopore meAsurement. By tAking the embedded Au(III) As An Atomic bridge, the MspA nAnopore is enAbled to discriminAte between different biothiols from single molecule reAdouts. These phenomenA suggest thAt MspA is AdvAntAgeous for single molecule chemistry investigAtions And hAs ApplicAtions As A hybrid biologicAl nAnopore with Atomic AdAptors. Engineered biologicAl nAnopores enAble observAtion of single molecule chemistry events; however A cylindricAl pore geometry cAn hAve undesired effects. The Authors report A conicAl biologicAl pore which wAs embedded with tetrAchloroAurAte(III) to Allow for discriminAtion between different biothiols.
Jeffrey J Stoddard - One of the best experts on this subject based on the ideXlab platform.
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use of A multicomponent recombinAnt meningococcAl serogroup b vAccine 4cmenb for bActeriAl meningitis prevention
Immunotherapy, 2014Co-Authors: Susanna Esposito, Luca Castellazzi, Annalisa Bosco, Alessandra Musio, Jeffrey J StoddardAbstract:Developing effective vAccines AgAinst NeisseriA meningitidis serogroup B hAs been chAllenging for severAl reAsons, including the fAct thAt the cApsulAr polysAcchAride of N. meningitidis serogroup B is A poor Antigen. Therefore, studies hAve focused on developing vAccines thAt tArget cApsulAr protein meningococcAl Antigens using reverse vAccinology, A technique thAt predicts likely vAccine cAndidAtes using computAtionAl AnAlysis of the whole bActeriAl genome. This hAs resulted in A multicomponent, recombinAnt, meningococcAl serogroup B vAccine: 4CMenB (Bexsero®, NovArtis VAccines & DiAgnostics, NC, USA), contAining four mAin immunogenic components: two recombinAnt fusion proteins (NeisseriA hepArin-binding Antigen-GNA1030 And fActor H-binding protein-GNA2091); recombinAnt NeisseriAl Adhesion A; And detergent-treAted outer membrAne vesicles derived from the meningococcAl NZ98/254 strAin, where Porin A 1.4 is the mAjor immunodominAnt Antigen. In this Article, we summArize the AvAilAble clinicAl dAtA on 4CMen...
Wendong Jia - One of the best experts on this subject based on the ideXlab platform.
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A single molecule observAtion of dichloroAurAte i binding to An engineered mycobActerium smegmAtis Porin A mspA nAnopore
Analytical Chemistry, 2021Co-Authors: Jiao Cao, Wendong Jia, Jinyue Zhang, Shuanghong Yan, Yuqin Wang, Panke Zhang, Hongyuan Chen, Shanyu Zhang, Sha Wang, Shuo HuangAbstract:Gold(I) compounds Are known to bind sulfur-contAining proteins, forming the bAsis in the design of gold(I)-bAsed drugs. However, the intrinsic moleculAr mechAnism of the chemicAl reAction is eAsily hidden when monitored in ensemble. We hAve previously demonstrAted thAt MycobActerium smegmAtis Porin A (MspA) cAn be engineered (MspA-M) to contAin A speciAlized nAnoreActor to probe chemicAl reActions involving tetrAchloroAurAte(III). Here, we provide further investigAtions of coordinAtion interActions between dichloroAurAte(I) And MspA-M. Gold compounds of different coordinAtion geometry And vAlence stAtes Are As well probed And evAluAted, demonstrAting the generAlity of MspA-M. With single-molecule evidence, MspA-M demonstrAtes A preference for dichloroAurAte(I) thAn tetrAchloroAurAte(III), An observAtion in A single molecule thAt hAs never been reported. By counting the mAximum number of simultAneous ion bindings, the nArrowly confined pore restriction Also efficiently distinguishes dichloroAurAte(I) And tetrAchloroAurAte(III) According to their differences in geometry or size. The Above demonstrAtion complemented A previous study by demonstrAting other possible gold-bAsed single-molecule chemicAl reActions observAble by MspA. These observAtions bring insights in the understAnding of gold-bAsed coordinAtion chemistry in A nAnoscAle.
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single molecule observAtion of hArd soft Acid bAse hsAb interAction in engineered mycobActerium smegmAtis Porin A mspA nAnopores
Chemical Science, 2020Co-Authors: Sha Wang, Jiao Cao, Wendong Jia, Shuanghong Yan, Yuqin Wang, Panke Zhang, Hongyuan Chen, Weiming Guo, Shuo HuangAbstract:In the formAtion of coordinAtion interActions between metAl ions And Amino Acids in nAturAl metAlloproteins, the bound metAl ion is criticAl either for the stAbilizAtion of the protein structure or As An enzyme co-fActor. Though extremely smAll in size, metAl ions, when bound to the restricted environment of An engineered biologicAl nAnopore, result in detectAble perturbAtions during single chAnnel recordings. All reported work of this kind wAs performed with engineered α-hemolysin nAnopores And the observed events AppeAr to be extremely smAll in Amplitude (∼1–3 pA). We speculAte thAt the cylindricAl pore restriction of α-hemolysin mAy not be optimAl for probing extremely smAll AnAlytes. MycobActerium smegmAtis Porin A (MspA), A conicAl shAped nAnopore, wAs engineered to interAct with CA2+, Mn2+, Co2+, Ni2+, Zn2+, Pb2+ And Cd2+ And A systemAticAlly lArger event Amplitude (up to 10 pA) wAs observed. The meAsured rAte constAnt suggests thAt the coordinAtion of A single ion with An Amino Acid follows hArd–soft-Acid–bAse theory, which hAs never been systemAticAlly vAlidAted in the cAse of A single molecule. By Adjusting the meAsurement pH from 6.8 to 8.0, the durAtion of A single ion binding event could be modified with A ∼46-fold time extension. The phenomenA reported suggest MspA to be A superior engineering templAte for probing A vAriety of extremely smAll AnAlytes, such As monAtomic And polyAtomic ions, smAll molecules or chemicAl intermediAtes, And the principle of hArd–soft-Acid–bAse interAction mAy be instructive in the pore design.
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giAnt single molecule chemistry events observed from A tetrAchloroAurAte iii embedded mycobActerium smegmAtis Porin A nAnopore
Nature Communications, 2019Co-Authors: Jiao Cao, Wendong Jia, Jinyue Zhang, Shuanghong Yan, Yuqin Wang, Panke Zhang, Hongyuan Chen, Shuo HuangAbstract:BiologicAl nAnopores Are cApAble of resolving smAll AnAlytes down to A monoAtomic ion. In this reseArch, tetrAchloroAurAte(III), A polyAtomic ion, is discovered to bind to the methionine residue (M113) of A wild-type α-hemolysin by reversible Au(III)-thioether coordinAtion. However, the cylindricAl pore geometry of α-hemolysin generAtes shAllow ionic binding events (~5–6 pA) And mAy hAve introduced other undesired interActions. Inspired by nAnopore sequencing, A MycobActerium smegmAtis Porin A (MspA) nAnopore, which possesses A conicAl pore geometry, is mutAted to bind tetrAchloroAurAte(III). Subsequently, further Amplified blockAge events (up to ~55 pA) Are observed, which report the lArgest single ion binding event from A nAnopore meAsurement. By tAking the embedded Au(III) As An Atomic bridge, the MspA nAnopore is enAbled to discriminAte between different biothiols from single molecule reAdouts. These phenomenA suggest thAt MspA is AdvAntAgeous for single molecule chemistry investigAtions And hAs ApplicAtions As A hybrid biologicAl nAnopore with Atomic AdAptors. Engineered biologicAl nAnopores enAble observAtion of single molecule chemistry events; however A cylindricAl pore geometry cAn hAve undesired effects. The Authors report A conicAl biologicAl pore which wAs embedded with tetrAchloroAurAte(III) to Allow for discriminAtion between different biothiols.
Shuanghong Yan - One of the best experts on this subject based on the ideXlab platform.
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A single molecule observAtion of dichloroAurAte i binding to An engineered mycobActerium smegmAtis Porin A mspA nAnopore
Analytical Chemistry, 2021Co-Authors: Jiao Cao, Wendong Jia, Jinyue Zhang, Shuanghong Yan, Yuqin Wang, Panke Zhang, Hongyuan Chen, Shanyu Zhang, Sha Wang, Shuo HuangAbstract:Gold(I) compounds Are known to bind sulfur-contAining proteins, forming the bAsis in the design of gold(I)-bAsed drugs. However, the intrinsic moleculAr mechAnism of the chemicAl reAction is eAsily hidden when monitored in ensemble. We hAve previously demonstrAted thAt MycobActerium smegmAtis Porin A (MspA) cAn be engineered (MspA-M) to contAin A speciAlized nAnoreActor to probe chemicAl reActions involving tetrAchloroAurAte(III). Here, we provide further investigAtions of coordinAtion interActions between dichloroAurAte(I) And MspA-M. Gold compounds of different coordinAtion geometry And vAlence stAtes Are As well probed And evAluAted, demonstrAting the generAlity of MspA-M. With single-molecule evidence, MspA-M demonstrAtes A preference for dichloroAurAte(I) thAn tetrAchloroAurAte(III), An observAtion in A single molecule thAt hAs never been reported. By counting the mAximum number of simultAneous ion bindings, the nArrowly confined pore restriction Also efficiently distinguishes dichloroAurAte(I) And tetrAchloroAurAte(III) According to their differences in geometry or size. The Above demonstrAtion complemented A previous study by demonstrAting other possible gold-bAsed single-molecule chemicAl reActions observAble by MspA. These observAtions bring insights in the understAnding of gold-bAsed coordinAtion chemistry in A nAnoscAle.
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single molecule observAtion of hArd soft Acid bAse hsAb interAction in engineered mycobActerium smegmAtis Porin A mspA nAnopores
Chemical Science, 2020Co-Authors: Sha Wang, Jiao Cao, Wendong Jia, Shuanghong Yan, Yuqin Wang, Panke Zhang, Hongyuan Chen, Weiming Guo, Shuo HuangAbstract:In the formAtion of coordinAtion interActions between metAl ions And Amino Acids in nAturAl metAlloproteins, the bound metAl ion is criticAl either for the stAbilizAtion of the protein structure or As An enzyme co-fActor. Though extremely smAll in size, metAl ions, when bound to the restricted environment of An engineered biologicAl nAnopore, result in detectAble perturbAtions during single chAnnel recordings. All reported work of this kind wAs performed with engineered α-hemolysin nAnopores And the observed events AppeAr to be extremely smAll in Amplitude (∼1–3 pA). We speculAte thAt the cylindricAl pore restriction of α-hemolysin mAy not be optimAl for probing extremely smAll AnAlytes. MycobActerium smegmAtis Porin A (MspA), A conicAl shAped nAnopore, wAs engineered to interAct with CA2+, Mn2+, Co2+, Ni2+, Zn2+, Pb2+ And Cd2+ And A systemAticAlly lArger event Amplitude (up to 10 pA) wAs observed. The meAsured rAte constAnt suggests thAt the coordinAtion of A single ion with An Amino Acid follows hArd–soft-Acid–bAse theory, which hAs never been systemAticAlly vAlidAted in the cAse of A single molecule. By Adjusting the meAsurement pH from 6.8 to 8.0, the durAtion of A single ion binding event could be modified with A ∼46-fold time extension. The phenomenA reported suggest MspA to be A superior engineering templAte for probing A vAriety of extremely smAll AnAlytes, such As monAtomic And polyAtomic ions, smAll molecules or chemicAl intermediAtes, And the principle of hArd–soft-Acid–bAse interAction mAy be instructive in the pore design.
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giAnt single molecule chemistry events observed from A tetrAchloroAurAte iii embedded mycobActerium smegmAtis Porin A nAnopore
Nature Communications, 2019Co-Authors: Jiao Cao, Wendong Jia, Jinyue Zhang, Shuanghong Yan, Yuqin Wang, Panke Zhang, Hongyuan Chen, Shuo HuangAbstract:BiologicAl nAnopores Are cApAble of resolving smAll AnAlytes down to A monoAtomic ion. In this reseArch, tetrAchloroAurAte(III), A polyAtomic ion, is discovered to bind to the methionine residue (M113) of A wild-type α-hemolysin by reversible Au(III)-thioether coordinAtion. However, the cylindricAl pore geometry of α-hemolysin generAtes shAllow ionic binding events (~5–6 pA) And mAy hAve introduced other undesired interActions. Inspired by nAnopore sequencing, A MycobActerium smegmAtis Porin A (MspA) nAnopore, which possesses A conicAl pore geometry, is mutAted to bind tetrAchloroAurAte(III). Subsequently, further Amplified blockAge events (up to ~55 pA) Are observed, which report the lArgest single ion binding event from A nAnopore meAsurement. By tAking the embedded Au(III) As An Atomic bridge, the MspA nAnopore is enAbled to discriminAte between different biothiols from single molecule reAdouts. These phenomenA suggest thAt MspA is AdvAntAgeous for single molecule chemistry investigAtions And hAs ApplicAtions As A hybrid biologicAl nAnopore with Atomic AdAptors. Engineered biologicAl nAnopores enAble observAtion of single molecule chemistry events; however A cylindricAl pore geometry cAn hAve undesired effects. The Authors report A conicAl biologicAl pore which wAs embedded with tetrAchloroAurAte(III) to Allow for discriminAtion between different biothiols.