Hirshfeld Surface and Structure Analysis of Two Co-crystal of Isonicotinic Acid Hydrazide / 医药导报

Objective Two co-crystals of isonicotinic acid hydrazide(INH)-malonic acid and INH-glutaric acid were prepared.The formation mechanism and intermolecular interaction were studied. Methods Three-dimensional structure of 2 co-crystals were obtained though single crystal X-ray diffraction(SXRD), and intermolecular interaction was analyzed using Hirshfeld surface method. Results INH-malonic acid crystalized in stoichiometric ratio of 1:0.5,while INH-glutaric acid in 1:1.Two co-crystals maintain their stable arrangement in space by hydrogen bond and van der Waals force. Conclusion With the existence of pyridine ring and carbohydrazide group in INH,which mainter-molecular interaction in co-crystal can be directly and clearly revealed by Hirshfeld surface analysis.

A Case of Anagen Effluvium Induced by INH (Isonicotinic Acid Hydrazide) / 대한피부과학회지

We report a case of a 30 year-old woman who presented with acute scalp hair loss induced by isonicotinic acid hydrazide gap (INH). Considerable hair loss started within 4 weeks of INH administration. There was no evidence of dermatitis, allergic reaction, or any other cause for the hair loss. INH was discontinued, and the hair loss stopped within 4 weeks, with new hair growth seen. There was complete recovery of hair loss after 12 weeks of alopecia. Medication-induced hair loss is an occasional adverse effect of many drugs, however hair loss induced by INH has been reported in only 1 case. The complete recovery from anagen effluvium is difficult to explain, but it could have been due to the early discontinuance of INH.

Effect of cupric-isonicotinic acid hydrazide complex on avian myeloblastosis virus reverse transcriptase and its associated enzyme activities.

Cupric complex of isonicotinic acid hydrazide inhibits DNA synthesis by avian myloblastosis virus reverse transcriptase. This inhibition occurs in the presence of either ribonucleotide or deoxyribonucleotide templates. The inhibition of reverse transcriptase by cupric-INH complex is considerably reduced when stored or proteolytically cleaved enzyme was used in the reaction. The complex also inhibits the reverse transciptase-associated RNase Η activity. The cupric-isonicotinic acid hydrazide complex cleaves pBR 322 from I DNA into smaller molecules in the presence or absence of reverse transcriptase-associated endonuclease. However, in the presence of the enzyme the DNA is cleaved to a greater extent.

Effect of cupric-isonicotinic acid hydrazide complex on normal and avian myeloblastosis virus-infected cells cultivated in vitro.

The cupric complex of isonicotinic acid hydrazide was found to be nontoxic to normal yolk sac macrophages upto a concentration of 100 μΜ. At this concentration the complex did not significantly inhibit DNA, RNA or protein synthesis in these cells. The complex inhibited the avian myeloblastosis virus multiplication in these cells when added 0–4 h post-infection as demonstrated by the inhibition of both focus formation and expression of viral specific antigens. This inhibition was not observed when the complex was added 8 and 16 h after avian myeloblastosis virus infection. The studies carried out on avian myeloblastosis virus-transformed myeloblasts indicated that the complex had no effect on the colony (focus) formation. The results suggest that the complex inhibits the virus multiplication by interfering in an early event of viral growth cycle, possibly the process of reverse transcription.