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PH-induced conformational changes in histamine in the solid state.

ABSTRACT: Histamine is one of the most basic biogenic amino-compounds, which is composed of imidazole and a flexible ethylamine side chain moiety. Histamine is known to take the form of various types of cations, free base, monocation and dication form, where its conformational change is highly sensitively to the pH conditions. The details of these changes are still controversial due to a lack of detailed information on its crystal structures. Thus, in this study, the molecular packing structures of histidine at various pH were analyzed via X-ray diffraction in combination with vibrational spectroscopy and energy calculations. A variety of molecular conformations including the tautomeric phenomenon was found to be intimately related with intra- and intermolecular hydrogen bonds. The role of the hydrogen bonds was studied also to check the possibility of high proton conductivity of histamine, as predicted by computer simulation. Consequently, the thus-predicted proton conductivity was confirmed for the first time experimentally. During the heating process, the conductivity showed the relatively high maximum value of 10^-4 S cm^-1 at around 60 °C, which is related to the effective proton transfer between the amino NH group of one histamine unit and the imidazole ring of another.

SUBMITTER: Kodchakorn K

PROVIDER: S-EPMC9065317 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature

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pH-induced conformational changes in histamine in the solid state.

Kodchakorn Kanchanok K Nimmanpipug Piyarat P Phongtamrug Suttinun S Tashiro Kohji K

RSC advances 20190620 34

Histamine is one of the most basic biogenic amino-compounds, which is composed of imidazole and a flexible ethylamine side chain moiety. Histamine is known to take the form of various types of cations, free base, monocation and dication form, where its conformational change is highly sensitively to the pH conditions. The details of these changes are still controversial due to a lack of detailed information on its crystal structures. Thus, in this study, the molecular packing structures of histid ...[more]

PMID: 35519396

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Project description:Human bocavirus 1 (HBoV1) and HBoV2-4 infect children and immunocompromised individuals, resulting in respiratory and gastrointestinal infections, respectively. Using cryo-electron microscopy and image reconstruction, the HBoV2 capsid structure was determined to 2.7 Å resolution at pH 7.4 and compared to the previously determined HBoV1, HBoV3, and HBoV4 structures. Consistent with previous findings, surface variable region (VR) III of the capsid protein VP3, proposed as a host tissue-tropism determinant, was structurally similar among the gastrointestinal strains HBoV2-4, but differed from HBoV1 with its tropism for the respiratory tract. Towards understanding the entry and trafficking properties of these viruses, HBoV1 and HBoV2 were further analyzed as species representatives of the two HBoV tropisms. Their cell surface glycan-binding characteristics were analyzed, and capsid structures determined to 2.5-2.7 Å resolution at pH 5.5 and 2.6, conditions normally encountered during infection. The data showed that glycans with terminal sialic acid, galactose, GlcNAc or heparan sulfate moieties do not facilitate HBoV1 or HBoV2 cellular attachment. With respect to trafficking, conformational changes common to both viruses were observed at low pH conditions localized to the VP N-terminus under the 5-fold channel, in the surface loops VR-I and VR-V and specific side-chain residues such as cysteines and histidines. The 5-fold conformational movements provide insight into the potential mechanism of VP N-terminal dynamics during HBoV infection and side-chain modifications highlight pH-sensitive regions of the capsid.IMPORTANCE Human bocaviruses (HBoVs) are associated with disease in humans. However, the lack of an animal model and a versatile cell culture system to study their life cycle limits the ability to develop specific treatments or vaccines. This study presents the structure of HBoV2, at 2.7 Å resolution, determined for comparison to the existing HBoV1, HBoV3, and HBoV4 structures, to enable the molecular characterization of strain and genus-specific capsid features contributing to tissue tropism and antigenicity. Furthermore, HBoV1 and HBoV2 structures determined under acidic conditions provide insight into capsid changes associated with endosomal and gastrointestinal acidification. Structural rearrangements of the capsid VP N-terminus, at the base of the 5-fold channel, demonstrate a disordering of a "basket" motif as pH decreases. These observations begin to unravel the molecular mechanism of HBoV infection and provide information for control strategies.

Dataset Information

PH-induced conformational changes in histamine in the solid state.

Publications

pH-induced conformational changes in histamine in the solid state.

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