Simon Aman

Neuropeptides are small protein-like molecules used by neurons to communicate with each other. Unlike classical neurotransmitters, which act quickly and locally, neuropeptides often produce slower but longer-lasting effects on brain function. They play a crucial role in regulating emotions, stress responses, and overall mental well-being. Increasing evidence shows that imbalances in neuropeptide systems are linked […]

The discovery of bioactive peptides has been greatly accelerated by the development of peptide libraries and high-throughput screening (HTS) techniques. These approaches allow researchers to generate and test thousands to millions of peptide sequences rapidly, identifying candidates with desired biological activities such as antimicrobial, anticancer, or receptor-binding properties. Together, peptide libraries and HTS form a

Peptide-based ingredients are widely used in modern cosmetics, particularly in anti-aging, skin-repair, and hair-care products. These bioactive compounds can stimulate collagen production, improve skin elasticity, and enhance overall skin appearance. However, because peptides can exert biological effects, their use in cosmetics raises important regulatory considerations. Ensuring safety, compliance, and accurate marketing is essential for manufacturers

The discovery and development of bioactive peptides have traditionally relied on experimental screening and trial-and-error approaches. However, these methods are time-consuming and resource-intensive. With the rise of artificial intelligence (AI) and computational biology, researchers can now design and optimize peptides more efficiently. AI-driven approaches are transforming peptide therapeutics by enabling rapid prediction of structure, function,

Structure–activity relationships (SAR) play a central role in the design and optimization of peptide therapeutics. SAR refers to the systematic study of how changes in a molecule’s structure influence its biological activity. In the context of peptides, this involves modifying amino acid sequences, chemical bonds, and overall conformation to enhance properties such as potency, selectivity,

Protein folding is a fundamental biological process, and short peptides provide a simplified model for understanding how folding occurs at the molecular level. Unlike large proteins, short peptides (typically 5–30 amino acids) have fewer interactions and structural constraints, making them ideal systems for studying the basic principles of folding. Insights gained from peptide folding mechanisms

Peptide-based biomaterials have gained significant attention in recent years due to their biocompatibility, tunability, and ability to mimic natural biological structures. Among these, peptide hydrogels and scaffolds are particularly important in tissue engineering, regenerative medicine, and drug delivery. These materials are formed through the self-assembly of peptides into organized structures, creating environments that support cell

Biofouling—the unwanted accumulation of microorganisms, algae, and marine organisms on surfaces—is a major challenge in both marine and industrial environments. It affects ship hulls, offshore structures, pipelines, water treatment systems, and medical devices. Traditional antifouling strategies often rely on toxic coatings, which can harm ecosystems and face increasing regulatory restrictions. In response, antifouling peptides have

The rapid rise of antibiotic-resistant bacteria has become one of the most serious global health threats. Traditional antibiotics are losing effectiveness due to overuse and misuse, leading to infections that are increasingly difficult to treat. In this context, antimicrobial peptides (AMPs) have emerged as promising alternatives. These naturally occurring molecules are part of the innate

Drug discovery has traditionally relied on small-molecule drugs, but peptide-based therapeutics are becoming increasingly important in modern medicine. Peptides, which are short chains of amino acids, lie between small molecules and large biologics in terms of size and complexity. Their unique properties allow them to interact with biological systems in ways that differ significantly from