Combined crystalline, lamellar and granular structural insights into in vitro digestion rate of native starches

2020 ◽  
Vol 105 ◽  
pp. 105823 ◽  
Author(s):  
Cheng Li ◽  
Bo Gong ◽  
Yiming Hu ◽  
Xingxun Liu ◽  
Xiao Guan ◽  
...  
LWT ◽  
2006 ◽  
Vol 39 (8) ◽  
pp. 947-951 ◽  
Author(s):  
José Juan Islas-Hernández ◽  
Rodolfo Rendón-Villalobos ◽  
Edith Agama-Acevedo ◽  
Felipe Gutiérrez-Meraz ◽  
Juscelino Tovar ◽  
...  

1971 ◽  
Vol 54 (1) ◽  
pp. 71-76 ◽  
Author(s):  
L.W. Smith ◽  
H.K. Goering ◽  
D.R. Waldo ◽  
C.H. Gordon

2014 ◽  
Vol 5 (11) ◽  
pp. 2686-2698 ◽  
Author(s):  
Tanoj K. Singh ◽  
Sofia K. Øiseth ◽  
Leif Lundin ◽  
Li Day

Protein intake is essential for growth and repair of body cells, the normal functioning of muscles, and health related immune functions.


2019 ◽  
Vol 10 (9) ◽  
pp. 5312-5322 ◽  
Author(s):  
Li Ding ◽  
Qiang Huang ◽  
Haiteng Li ◽  
Zhigang Wang ◽  
Xiong Fu ◽  
...  

The starch digestion rate and extent of potato-based food were modulated through controlled gelatinization.


Author(s):  
Parth Sarthi Sen Gupta ◽  
Satyaranjan Biswal ◽  
Saroj Kumar Panda ◽  
Abhik Kumar Ray ◽  
Malay Kumar Rana

<p>While an FDA approved drug Ivermectin was reported to dramatically reduce the cell line of SARS-CoV-2 by ~5000 folds within 48 hours, the precise mechanism of action and the COVID-19 molecular target involved in interaction with this in-vitro effective drug are unknown yet. Among 12 different COVID-19 targets studied here, the RNA dependent RNA polymerase (RdRp) with RNA and Helicase NCB site show the strongest affinity to Ivermectin amounting -10.4 kcal/mol and -9.6 kcal/mol, respectively. Molecular dynamics of corresponding protein-drug complexes reveals that the drug bound state of RdRp with RNA has better structural stability than the Helicase NCB site, with MM/PBSA free energy of -135.2 kJ/mol, almost twice that of Helicase (-76.6 kJ/mol). The selectivity of Ivermectin to RdRp is triggered by a cooperative interaction of RNA-RdRp by ternary complex formation. Identification of the target and its interaction profile with Ivermectin can lead to more powerful drug designs for COVID-19 and experimental exploration. </p>


2020 ◽  
Vol 328 ◽  
pp. 127126 ◽  
Author(s):  
Stefano Nebbia ◽  
Marzia Giribaldi ◽  
Laura Cavallarin ◽  
Enrico Bertino ◽  
Alessandra Coscia ◽  
...  

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