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Aparna Rachamallu
Researcher at University of Hyderabad
Publications - 12
Citations - 606
Aparna Rachamallu is an academic researcher from University of Hyderabad. The author has contributed to research in topics: Human serum albumin & Binding constant. The author has an hindex of 9, co-authored 12 publications receiving 533 citations.
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Molecular mechanisms in C-Phycocyanin induced apoptosis in human chronic myeloid leukemia cell line-K562.
Jagu Subhashini,Suraneni V.K. Mahipal,Madhava C. Reddy,Metukuri Mallikarjuna Reddy,Aparna Rachamallu,Pallu Reddanna +5 more
TL;DR: It is demonstrated that C-PC induces apoptosis in K562 cells by cytochrome c release from mitochondria into the cytosol, PARP cleavage and down regulation of Bcl-2.
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Binding and molecular dynamics studies of 7-hydroxycoumarin derivatives with human serum albumin and its pharmacological importance.
Daniel Pushparaju Yeggoni,Mahesh Gokara,Darla Mark Manidhar,Aparna Rachamallu,Sailaja Nakka,Cirandur Suresh Reddy,Rajagopal Subramanyam +6 more
TL;DR: These studies revealed that 7-hydroxycoumarin derivatives caused an increased inhibition in growth of inflamed macrophages in a concentration-dependent manner with an IC50 of 78, 63, and 50 μM, suggesting that there are hydrophobic interactions when coumarin derivative-inspired drugs bind to HSA.
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Cytotoxicity and comparative binding mechanism of piperine with human serum albumin and α-1-acid glycoprotein
TL;DR: The binding constants and free energy corresponding to experimental and computational analysis suggest that there are hydrophobic and hydrophilic interactions when piperine binds to HSA and AGP and prove that the HSA–piperine complex is stable in nature.
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A comparative binding mechanism between human serum albumin and α-1-acid glycoprotein with corilagin: biophysical and computational approach
TL;DR: This study reveals that corilagin caused an increase in inhibition growth of inflamed macrophages in concentration-dependent manner with an IC50 value of 66 μM, which proves that the HSA–corilagin complex is stable in nature.
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Elucidating the binding interaction of andrographolide with the plasma proteins: biophysical and computational approach
TL;DR: The results provide evidence that both plasma proteins (HSA and AGP) can act as carrier proteins for ANDR, and molecular dynamics simulation revealed that the stability of the HSA–ANDR complexes reached an equilibration state at around 3000 ps, which clearly indicates the rigidity and stability of.