Nanoparticles Could Help in Screening Individuals for Thalassaemia

A type of nanoparticles could provide clues to whether a person carries the defective gene for thalassaemia, claims a research team from Kolkata-based Calcutta University. Known as copper nanoparticles (CuNPs), the nanomolecules form various protein aggregates binding to haemoglobin, the metalloprotein in red blood cells. Besides protein aggregrates, the copper nanoparticles also precipitate the aggregated protein.

The researchers found that the nanoparticles formed a distinct aggregation when bound to a mutated form of haemoglobin that leads to beta-thalassaemia. Using special techniques like atomic absorption spectroscopy and high-pressure liquid chromatography, the team found the nanoparticles were co-precipitated with specific variants of haemoglobin. Studies showed that protein initially broke the nanoclusters into smaller sizes (4nm), followed by gradual increase in cluster size. A suitable scaling up of the approach may have important implications in screening haemoglobinopathies such beta-thalassaemia, write the researchers in a recent issue of Nanomedicine.

According to an estimate, there would be about 45 million carriers and about 15,000 infants born each year with haemoglobinopathies in India. The carrier frequency of haemoglobinopathy varies from 3 to 17 per cent in different population groups of India. In India, beta-thalassaemia comprises about 80–90 per cent of the total thalassaemias reported. More than 200 beta-thalassaemia mutations have been identified all over the world and of these about 28 mutations have been documented in Indian patients. There is growing concern that thalassemia may become a very serious problem in the next 50 years.

Antidote to Infertility from Buffalo Blood

A protein isolated from buffalo blood induces forward motility of goat sperm, en essential quality that makes fertilisation possible in animals and humans, claims a research team from the Indian Institute of Chemical Biology, Kolkata. Known as the forward motility stimulating factor (FMSF), it has been shown to activate goat spermatozoa.

“FMSF can be used to enhance fertility in animal breeding farms and human infertility clinics,” says Gopal Chandra Majumder, the lead author. “The motility-promoting efficacy of FMSF is higher than non-protein activators like theophylline and bicarbonate. Besides, it is not species specific,” Majumder adds. FMSF, according to him, also has the potential for improving breeding of wild animals, and should help species that are almost extinct or endangered.

After isolation from buffalo blood fluid, FMSF was purified and exposed to goat sperm incubated in plasma. The team found two types of FMSF (FMSF-I, FMSF-II). Nearly 20-30 per cent goat spermatozoa showed forward progression in the absence of FMSF-I. The addition of it enhanced sperm forward motility significantly.

“The motility-promoting action is nearly complete in about one minute compared to other motility-promoting factors (theophylline and bicarbonate), which take six minutes to initiate maximal forward motility of sperm,” says Majumder. Mostly synthesized in liver, FMSF-I stimulates the motility of sperm of goat, rat, and humans. This shows that it has a certain regulatory role on sperm physiology. FMSF-I contains protein and sugar, both of which contribute to its motility-promoting factor, he says.

“Study reveals that FMSF-I binds to the receptor protein on sperm cell surface, which activates a second messenger protein, which in turn triggers a cascade of cellular events inside the sperm inducing forward motility,” explains Majumder in a paper published in the November issue of Journal of cellular Physiology (Vol 209, No 2).

The above article was originally published in ‘Down to Earth’, a science and fortnightly published from New Delhi and originally written by this blogger.

Scientists Snap an Image of a Piece of HIV Protein

In a groundbreaking discovery, for the first time researchers from the National Institute of Allergy and Infections Diseases (part of National Institutes of Health), Dana-Farber Cancer Institute in Boston, and The Scripps Research Institute in La Jolla have crystallized and captured an atomic-level picture of a key portion of an HIV surface protein as it looks when bound to an infection-fighting antibody. Unlike much of the constantly mutating virus, this protein component is stable and -- more importantly, say the researchers -- appears vulnerable to attack from this specific antibody, known as b12, which can broadly neutralize HIV.

This finding, one of the best leads to come along in years, shows us a critical area of vulnerability on the virus that may be used to target with vaccines, sum up the researchers.


This neutralizing antibody binds to a HIV surface protein called gp120. Until now, no one had succeeded in determining the detailed structure of b12 in complex with gp120. It was extremely difficult to crystallize b12 bound to gp120, say the researchers in the 15 February online issue of Nature, in part due to the inherently flexible nature of the chemical bonds in gp120. To overcome the problem, the investigators created a variety of gp120s and eventually made the protein stiff enough to capture a picture of it in complex with b12. They saw that b12 binds gp120 at the same point where gp120 initially attaches to CD4 (a type of host’s cell surface protein).