Narrow Results

A novel nanofabrication method that combines both "bottom-up" (template-assisted peptide self-assembling) and "top-down" (replica molding) techniques is introduced. A designer peptide, GAV-9 (NH₂-VGGAVVAGV-CONH₂), can epitaxially self-assemble into nanofilaments on the surface of mica, which is further used as the diversified masters for the application of replica molding. With in situ atomic force microscopy monitoring, several typical masters are fabricated by peptide self-assembling on the surface of mica. These masters can be easily molded into hard poly(dimethylsiloxane) surfaces, and then further replica-molded into polyurethane surfaces. The polymeric surfaces with regular 1D and 2D patterns on the nanometer scale are expected to have new applications in nanostructure's fabrication.

Common Epilepsy Gene Discovered.

Peptide Found May Eliminate Anthrax.

Strong Demand for AEDs in Japan.

Fast Antibodies Peptide Mapping Solution from Agilent.

Thomson to Acquire Information Holdings.

Agilent Technologies licenses SureFISH to BioDiscovery.

Bionomics acquires US-based cancer stem cell company Eclipse Therapeutics.

AB SCIEX announces Biologics Initiative.

Phylogica licences skin-repair peptide to Le Métier De Beauté for cosmetic market.

Brooks' Single-use REMP tubes support optimization of automated serum and plasma storage

Genetic Technologies announces key managerial appointment Mark Ostrowski to head-up US sales for BREVAGen™.

BioScience Managers banks on growth of anti-infectives market.

Rodin Therapeutics applies insights of epigenetics to neurological disorders.

LBT Innovations finalizes joint venture to drive global production of world-class automated diagnostics technology.

Phylogica expands collaborations with Janssen for peptide-drug conjugates.

Immune Design and Medicago announce license agreement and collaboration to develop novel adjuvanted pandemic influenza vaccines.

Bayat Foundation inaugurates new pediatric critical care facility at Indira Gandhi Hospital in Kabul.

The International Peptide Symposium Held in Singapore for the First Time.

Inspirations from 2015 FWIS L'Oréal Winners.

Emerging Opportunities in Myanmar's Diagnostic Imaging and In Vitro Diagnostics.

High-Throughput Sequencing on a Next Generation Sequencer to Identify Specific Binders from a Phage Library

Antibody Solution Viscosity and Intermolecular Interactions: Considerations for Development of Highly Concentrated Formulations

Display of Membrane Proteins on a Viral Envelope for Antibody Generation

Sequence and Structural Determinants of Antigen Binding in Antibody CDR Loops

Enhancement of the Stability of Single Chain Fv Molecules with the Amino Acid Substitutions Predicted by High-Performance Computer

Thermal Stability of Camelid Single Domain VHH Antibody

Amyloids are stable, β-sheet-rich protein/peptides aggregates with 2–15 nm diameter and few micrometers long. It is originally associated with many human diseases such as Alzheimer's, Parkinson's and prion diseases. Amyloids are resistant to enzyme degradation, temperature changes and wide ranges of pH. Although, amyloids are hard and their stiffness is comparable to steel, a constant recycling of monomer occur inside the amyloid fibrils. It grows in a nucleation dependent polymerization manner by recruiting native soluble protein and by converting them to amyloid. These extraordinary physical properties make amyloids attractive for nanotechnological applications. Some amyloid fibrils have also evolved to perform native biological functions (functional amyloid) of the host organism. Functional amyloids are present in mammals such as amyloids of pMel17 and pituitary hormones, where they help in skin pigmentation and hormone storage, respectively. Here, the progress of utilizing amyloid fibrils for nanobiotechnological applications with particular emphasis on the recent studies that amyloid could be utilized for the formulation of peptide/protein drugs depot and how secretory cells uses amyloid for hormone storage will be reviewed.

Helices are ubiquitous in art and nature. Independent of their pitch and sense of rotation (handedness), helices in sculpture, painting, architecture, scientific illustrations, conference announcements, logos, and advertising are eye-catching and aesthetically pleasing. Helices can turn either clockwise (right-handed helix) or anti-clockwise (left-handed helix). The $\alpha$-helix formed by l-amino acids and the double helices formed by $\beta$-d-2^′-deoxyribonucleic acid (A- and B-form DNA) and $\beta$-d-ribonucleic acid (A-form RNA) are all right-handed. Artistic license provides the freedom to create helices of any shape and sense; indeed, many helical sculptures do not follow the natural convention observed in proteins and DNA. What is more surprising, given that models of the $\alpha$-helix and the DNA double helix were published over 70 years ago, is how common left-handed DNA double helices are in the context of scientific papers and books as well as in popular science writing and reporting. In all cases except for left-handed Z-DNA, the use of left-handed helices in scientific illustrations or models is incorrect. Here, we revisit the helix types adopted by peptides, DNA, and RNA, and review examples of right and wrong helical models in science, art, and elsewhere.