Insulin resistance as well as insulin deficiency are said to be principal to the development of type 2 diabetes mellitus (T2Dm). Heme has also been suggested to play an important role in the disease etiology since many of the heme deficiency symptoms constitute the common pathological features of T2Dm. Besides, iron overload, higher heme iron intake and transfusion requiring diseases are associated with a higher risk of T2Dm development. In this study the interaction between these two key components [Formula: see text]. heme and insulin has been studied spectroscopically under different conditions which include the effect of excess peptide as well as increasing pH. The resultant heme-insulin complexes in their reduced state are found to produce very little partially reduced oxygen species (PROS) on getting oxidized by molecular oxygen. The interaction between insulin and previously reported T2Dm relevant heme-amylin complex were also examined using absorption and resonance Raman spectroscopy. The corresponding data suggest that insulin sequesters heme from heme-amylin to form the much less cytotoxic heme-insulin.
Colocalization of heme rich deposits in the senile plaque of Aβ in the cerebral cortex of Alzheimer’s disease (AD) brain along with altered heme homeostasis and heme deficiency symptoms in...
Amyloid β (Aβ)
peptides mutated at different positions
using a cysteine moiety assemble on Au electrodes using the thiol
functionality of cysteine. Self-assembled monolayers (SAMs) of Aβ
on Au surfaces can act as abiological platforms that allow the mimicking
of fibrils and oligomeric Aβ via the formation of controlled
large and small peptide aggregates. These Aβ constructs bind
with heme and Cu and exhibit different reactivities. These abiological
platforms can also be used to investigate potential drugs that can
interact with heme and Cu-Aβ. SAM formation of Aβ mutants
allows the study of different morphology and structure as well as
behavior changes on binding with different metals and cytochrome
c
(Cyt
c
). This review provides a detailed
insight into the structure and reactivities of various Aβ aggregated
on Au electrodes mimicking the cell membrane.
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