@article {44088,
	title = {Dendrimeric amide- and carbamate-linked lysine-based efficient molecular transporters},
	journal = {Organic \& Biomolecular Chemistry},
	volume = {15},
	year = {2017},
	month = {DEC},
	pages = {9579-9584},
	type = {Article},
	abstract = {<p>Amide- and carbamate-linked dendrimeric oligomers are reported as molecular transporters. They effectively complex with pDNA and transport it into cells at an efficiency superior to Lipofectamine, when complexation is carried out by incubation overnight. The carbamate-linked K2C is superior to amide-linked K2A; their pDNA complexes have very low associated cytotoxicity.</p>},
	doi = {10.1039/c7ob02552a},
	author = {Yadav, Amit Kumar and Dey, Namit and Chattopadhyay, Sabyasachi and Ganguli, Munia and Fernandes, Moneesha}
}
@article {49345,
	title = {Discovery of free glycated amines and glycated urea in diabetic plasma: potential implications in diabetes},
	journal = {ACS Omega},
	volume = {9},
	year = {2024},
	month = {MAY },
	pages = {24907-24915},
	type = {Article},
	abstract = {<p>
	The role of protein glycation in the pathogenesis of diabetes has been well established. Akin to proteins, free amino acids and other small-molecule amines are also susceptible to glycation in hyperglycemic conditions and may have a role in the pathogenesis of the disease. However, information about glycation of free amino acids and other small-molecule amines is relatively obscure. In the quest to discover small-molecule glycated amines in the plasma, we have synthesized glycated amino acids, glycated creatine, and glycated urea, and by using a high-resolution accurate mass spectrometer, a mass spectral library was developed comprising the precursor and predominant fragment masses of glycated amines. Using this information, we report the discovery of the glycation of free lysine, arginine, and leucine/isoleucine from the plasma of diabetic patients. This has great physiological significance as glycation of these amino acids may create their deficiency and affect vital physiological processes such as protein synthesis, cell signaling, and insulin secretion. Also, these glycated amino acids could serve as potential markers of diabetes and its complications. While other amines, such as creatinine and urea, accumulate in the plasma and act as biomarkers of diabetic nephropathy. For the first time, we report the detection of glycated urea in diabetic plasma, which is confirmed by matching the precursor and fragment masses with the in vitro synthesized glycated urea by using C-12(6) and C-13(6)-glucose. Further, we quantified glycated urea detected in two forms, monoglycated urea (MGU) and diglycated urea (DGU), by a targeted mass spectrometric approach in the plasma of healthy, diabetic, and diabetic nephropathy subjects. Both MGU and DGU showed a positive correlation with clinical parameters, such as blood glucose and HbA1c. Given that urea gets converted to glycated urea in hyperglycemic conditions, it is crucial to quantify MGU and DGU along with the urea for the diagnosis of diabetic nephropathy and study their physiological role in diabetes.</p>
},
	issn = {2470-1343},
	doi = {10.1021/acsomega.4c01772},
	author = {Shaikh, Rashdajabeen Q. and Das, Sancharini and Chaurasiya, Arvindkumar and Ashtamy, Murali G. and Sheikh, Amreen B. and Fernandes, Moneesha and Tiwari, Shalbha and Unnikrishnan, Ambika G. and Kulkarni, Mahesh J.}
}
