SGLT2 and DPP4 inhibitors improve Alzheimer's disease-like pathology and cognitive function through distinct mechanisms in a T2D-AD mouse model
Biomed Pharmacother. 2023 Oct 20;168:115755. doi: 10.1016/j.biopha.2023.115755. Online ahead of print.ABSTRACTAlzheimer's disease (AD) and type 2 diabetes mellitus (T2D) share common features, including insulin resistance. Brain insulin resistance has been implicated as a key factor in the pathogenesis of AD. Recent studies have demonstrated that anti-diabetic drugs sodium-glucose cotransporter-2 inhibitor (SGLT2-i) and dipeptidyl peptidase-4 inhibitor (DPP4-i) improve insulin sensitivity and provide neuroprotection. However, the effects of these two inhibitors on the brain metabolism and insulin resistance remain uninvest...
Source: Biomedicine and pharmacotherapy = Biomedecine and pharmacotherapie - October 23, 2023 Category: Drugs & Pharmacology Authors: A Young Sim Da Hyun Choi Jong Youl Kim Eun Ran Kim A-Ra Goh Yong-Ho Lee Jong Eun Lee Source Type: research
SGLT2 and DPP4 inhibitors improve Alzheimer's disease-like pathology and cognitive function through distinct mechanisms in a T2D-AD mouse model
Biomed Pharmacother. 2023 Oct 20;168:115755. doi: 10.1016/j.biopha.2023.115755. Online ahead of print.ABSTRACTAlzheimer's disease (AD) and type 2 diabetes mellitus (T2D) share common features, including insulin resistance. Brain insulin resistance has been implicated as a key factor in the pathogenesis of AD. Recent studies have demonstrated that anti-diabetic drugs sodium-glucose cotransporter-2 inhibitor (SGLT2-i) and dipeptidyl peptidase-4 inhibitor (DPP4-i) improve insulin sensitivity and provide neuroprotection. However, the effects of these two inhibitors on the brain metabolism and insulin resistance remain uninvest...
Source: Biomedicine and pharmacotherapy = Biomedecine and pharmacotherapie - October 23, 2023 Category: Drugs & Pharmacology Authors: A Young Sim Da Hyun Choi Jong Youl Kim Eun Ran Kim A-Ra Goh Yong-Ho Lee Jong Eun Lee Source Type: research
Differential effect of gastric bypass versus sleeve gastrectomy on insulinotropic action of endogenous incretins
CONCLUSIONS: After GB, increasing incretin activity augments prandial β-cell response whereas the β-cell sensitivity to increasing plasma concentrations of endogenous incretin is diminished.PMID:37853989 | DOI:10.1002/oby.23872 (Source: Obesity)
Source: Obesity - October 19, 2023 Category: Eating Disorders & Weight Management Authors: Marzieh Salehi Richard Peterson Devjit Tripathy Samantha Pezzica Ralph DeFronzo Amalia Gastaldelli Source Type: research
Differential effect of gastric bypass versus sleeve gastrectomy on insulinotropic action of endogenous incretins
CONCLUSIONS: After GB, increasing incretin activity augments prandial β-cell response whereas the β-cell sensitivity to increasing plasma concentrations of endogenous incretin is diminished.PMID:37853989 | DOI:10.1002/oby.23872 (Source: Obesity)
Source: Obesity - October 19, 2023 Category: Eating Disorders & Weight Management Authors: Marzieh Salehi Richard Peterson Devjit Tripathy Samantha Pezzica Ralph DeFronzo Amalia Gastaldelli Source Type: research
Clinical Features, Cardiovascular Risk Profile, and Therapeutic Trajectories of Patients with Type 2 Diabetes Candidate for Oral Semaglutide Therapy in the Italian Specialist Care
ConclusionThe study supports the potential of early implementation of oral semaglutide as a strategy to overcome therapeutic inertia and enhance T2D management. (Source: Diabetes Therapy)
Source: Diabetes Therapy - October 18, 2023 Category: Endocrinology Source Type: research
Mechanism of molecular interaction of sitagliptin with human DPP < sub > 4 < /sub > enzyme - New Insights
CONCLUSION: The stable interaction between the sitagliptin ligand and the DPP4 enzyme was demonstrated through molecular docking simulations. The findings presented in this work enhance the understanding of the physicochemical properties of the sitagliptin interaction site, supporting the design of more efficient gliptin-like iDPP4 inhibitors.PMID:37837799 | DOI:10.1016/j.advms.2023.10.002 (Source: Molecular Medicine)
Source: Molecular Medicine - October 14, 2023 Category: Molecular Biology Authors: Michelangelo Bauwelz Gonzatti Jos é Edvar Monteiro Júnior Ant ônio José Rocha Jonathas Sales de Oliveira Ant ônio José de Jesus Evangelista F átima Morgana Pio Fonseca V ânia Marilande Ceccatto Aricl écio Cunha de Oliveira Jos é Ednésio da Cruz Source Type: research
Mechanism of molecular interaction of sitagliptin with human DPP < sub > 4 < /sub > enzyme - New Insights
CONCLUSION: The stable interaction between the sitagliptin ligand and the DPP4 enzyme was demonstrated through molecular docking simulations. The findings presented in this work enhance the understanding of the physicochemical properties of the sitagliptin interaction site, supporting the design of more efficient gliptin-like iDPP4 inhibitors.PMID:37837799 | DOI:10.1016/j.advms.2023.10.002 (Source: Advances in Medical Sciences)
Source: Advances in Medical Sciences - October 14, 2023 Category: Biomedical Science Authors: Michelangelo Bauwelz Gonzatti Jos é Edvar Monteiro Júnior Ant ônio José Rocha Jonathas Sales de Oliveira Ant ônio José de Jesus Evangelista F átima Morgana Pio Fonseca V ânia Marilande Ceccatto Aricl écio Cunha de Oliveira Jos é Ednésio da Cruz Source Type: research
Mechanism of molecular interaction of sitagliptin with human DPP < sub > 4 < /sub > enzyme - New Insights
CONCLUSION: The stable interaction between the sitagliptin ligand and the DPP4 enzyme was demonstrated through molecular docking simulations. The findings presented in this work enhance the understanding of the physicochemical properties of the sitagliptin interaction site, supporting the design of more efficient gliptin-like iDPP4 inhibitors.PMID:37837799 | DOI:10.1016/j.advms.2023.10.002 (Source: Molecular Medicine)
Source: Molecular Medicine - October 14, 2023 Category: Molecular Biology Authors: Michelangelo Bauwelz Gonzatti Jos é Edvar Monteiro Júnior Ant ônio José Rocha Jonathas Sales de Oliveira Ant ônio José de Jesus Evangelista F átima Morgana Pio Fonseca V ânia Marilande Ceccatto Aricl écio Cunha de Oliveira Jos é Ednésio da Cruz Source Type: research
Mechanism of molecular interaction of sitagliptin with human DPP < sub > 4 < /sub > enzyme - New Insights
CONCLUSION: The stable interaction between the sitagliptin ligand and the DPP4 enzyme was demonstrated through molecular docking simulations. The findings presented in this work enhance the understanding of the physicochemical properties of the sitagliptin interaction site, supporting the design of more efficient gliptin-like iDPP4 inhibitors.PMID:37837799 | DOI:10.1016/j.advms.2023.10.002 (Source: Advances in Medical Sciences)
Source: Advances in Medical Sciences - October 14, 2023 Category: Biomedical Science Authors: Michelangelo Bauwelz Gonzatti Jos é Edvar Monteiro Júnior Ant ônio José Rocha Jonathas Sales de Oliveira Ant ônio José de Jesus Evangelista F átima Morgana Pio Fonseca V ânia Marilande Ceccatto Aricl écio Cunha de Oliveira Jos é Ednésio da Cruz Source Type: research
Mechanism of molecular interaction of sitagliptin with human DPP < sub > 4 < /sub > enzyme - New Insights
CONCLUSION: The stable interaction between the sitagliptin ligand and the DPP4 enzyme was demonstrated through molecular docking simulations. The findings presented in this work enhance the understanding of the physicochemical properties of the sitagliptin interaction site, supporting the design of more efficient gliptin-like iDPP4 inhibitors.PMID:37837799 | DOI:10.1016/j.advms.2023.10.002 (Source: Advances in Medical Sciences)
Source: Advances in Medical Sciences - October 14, 2023 Category: Biomedical Science Authors: Michelangelo Bauwelz Gonzatti Jos é Edvar Monteiro Júnior Ant ônio José Rocha Jonathas Sales de Oliveira Ant ônio José de Jesus Evangelista F átima Morgana Pio Fonseca V ânia Marilande Ceccatto Aricl écio Cunha de Oliveira Jos é Ednésio da Cruz Source Type: research
Mechanism of molecular interaction of sitagliptin with human DPP < sub > 4 < /sub > enzyme - New Insights
CONCLUSION: The stable interaction between the sitagliptin ligand and the DPP4 enzyme was demonstrated through molecular docking simulations. The findings presented in this work enhance the understanding of the physicochemical properties of the sitagliptin interaction site, supporting the design of more efficient gliptin-like iDPP4 inhibitors.PMID:37837799 | DOI:10.1016/j.advms.2023.10.002 (Source: Advances in Medical Sciences)
Source: Advances in Medical Sciences - October 14, 2023 Category: Biomedical Science Authors: Michelangelo Bauwelz Gonzatti Jos é Edvar Monteiro Júnior Ant ônio José Rocha Jonathas Sales de Oliveira Ant ônio José de Jesus Evangelista F átima Morgana Pio Fonseca V ânia Marilande Ceccatto Aricl écio Cunha de Oliveira Jos é Ednésio da Cruz Source Type: research
Mechanism of molecular interaction of sitagliptin with human DPP < sub > 4 < /sub > enzyme - New Insights
CONCLUSION: The stable interaction between the sitagliptin ligand and the DPP4 enzyme was demonstrated through molecular docking simulations. The findings presented in this work enhance the understanding of the physicochemical properties of the sitagliptin interaction site, supporting the design of more efficient gliptin-like iDPP4 inhibitors.PMID:37837799 | DOI:10.1016/j.advms.2023.10.002 (Source: Advances in Medical Sciences)
Source: Advances in Medical Sciences - October 14, 2023 Category: Biomedical Science Authors: Michelangelo Bauwelz Gonzatti Jos é Edvar Monteiro Júnior Ant ônio José Rocha Jonathas Sales de Oliveira Ant ônio José de Jesus Evangelista F átima Morgana Pio Fonseca V ânia Marilande Ceccatto Aricl écio Cunha de Oliveira Jos é Ednésio da Cruz Source Type: research
Mechanism of molecular interaction of sitagliptin with human DPP < sub > 4 < /sub > enzyme - New Insights
CONCLUSION: The stable interaction between the sitagliptin ligand and the DPP4 enzyme was demonstrated through molecular docking simulations. The findings presented in this work enhance the understanding of the physicochemical properties of the sitagliptin interaction site, supporting the design of more efficient gliptin-like iDPP4 inhibitors.PMID:37837799 | DOI:10.1016/j.advms.2023.10.002 (Source: Advances in Medical Sciences)
Source: Advances in Medical Sciences - October 14, 2023 Category: Biomedical Science Authors: Michelangelo Bauwelz Gonzatti Jos é Edvar Monteiro Júnior Ant ônio José Rocha Jonathas Sales de Oliveira Ant ônio José de Jesus Evangelista F átima Morgana Pio Fonseca V ânia Marilande Ceccatto Aricl écio Cunha de Oliveira Jos é Ednésio da Cruz Source Type: research
Designing a novel (R)- ω-transaminase for asymmetric synthesis of sitagliptin intermediate via motif swapping and semi-rational design
This study underscores a useful evolution strategy of engineering biocatalysts to confer new properties and functions on enzymes for synthesizing high-value drug intermediates.PMID:37820904 | DOI:10.1016/j.ijbiomac.2023.127348 (Source: International Journal of Biological Macromolecules)
Source: International Journal of Biological Macromolecules - October 11, 2023 Category: Biochemistry Authors: Fang-Ying Zhu Meng-Yu Huang Ken Zheng Xiao-Jian Zhang Xue Cai Liang-Gang Huang Zhi-Qiang Liu Yu-Guo Zheng Source Type: research
