High-throughput small-angle X-ray scattering (SAXS) enables early viscosity prediction of high-concentration monoclonal antibody (mAb) formulations by detecting self-association at dilute concentrations. Synchrotron SAXS was applied to 22 mAbs, revealing low-q upturns below 10 mg/mL for high-viscosity candidates. A classification based on structure factor transitions accurately distinguished high- and low-viscosity mAbs. This SAXS-based method offers a scalable, sample-efficient alternative to traditional, volume-intensive viscosity measurements.

NADES typically contain natural metabolites such as sugar, sugar alcohols and amino acids. We have developed methods of prescreening candidate NADES forming molecules and then using quantum chemical modeling (COSMO-RS) to predict the phase behavior of NADES forming combinations. In addition, characterization of the NADES at low temperatures will be discussed as well as applications for NADES across a variety of applications including protein stabilization, cryopreservation and de-icing/anti-icing applications. 

Advanced NMR techniques provide critical insights into the solution behavior of novel biologics, particularly under high-concentration conditions relevant to therapeutic formulations. We will highlight how NMR reveals aggregation, conformational stability, and molecular interactions that impact developability and shelf-life. These insights help address key formulation challenges, enabling the design of stable, effective biologic drugs.

Protein drug products offer high specificity and potency but face a major challenge: aggregation, which can compromise safety and efficacy. This study evaluates Hydroxypropyl-β-cyclodextrin (HPβCD) as an excipient to reduce both soluble and insoluble aggregation by stabilizing protein conformation and mitigating interfacial stress. Using six protein formulations under various storage and stress conditions, we assessed HPβCD’s impact on aggregation and explored its mechanisms through experimental and in silico modeling.

This presentation addresses the challenges of developing stable, high-concentration mAb formulations, where protein-protein interactions increase viscosity and affect stability and injectability. Using minimal-sample techniques (DLS,DWS, and NanovisQ), it examines how pH, salt type, and temperature influence aggregation behavior and rheological properties. The findings provide actionable insights into how formulation variables can be turned to control aggregation and improve product stability.

Tulane University has developed a cuvette-based spectroscopic platform providing comprehensive formulation data on the stability and aggregation of biologics. By enabling real-time monitoring of protein, peptide, or other biologic aggregation under a continuous excipient concentration gradient, researchers can identify optimal formulation parameters to support formulation development and optimization. This  presents an overview of the technology’s design and capabilities, and summarizes key market research findings on its applications in biologic drug development.

This recent cuvette-based technology allows characterizing of biologics and their stability, critical for formulation optimization, including avoidance of aggregation. It encompasses two technologies; i) monitoring the effects on biologics, including their reversibility, as agents are dialyzed in or out; these latter include electrolytes, surfactants, denaturants, and other excipients, and ii) measuring Molecular Weight, virial coefficients (A2, B22), kD for diffusion coefficients, CMC, and dissolution rates using automatic continuous dilution. The cuvette technology can be used in any spectroscopic instrument that accepts a 1 cm pathlength cuvette, without any need for modifications. Additionally, samples can be recovered following analysis.

A new device and methodology spectroscopically monitor how biologics behave as formulation conditions change continuously using dialysis. This allows rapid, real-time determination of regions of biologic stability as the concentrations of electrolytes, surfactants, and other excipients vary. Using complete dialysis cycles the reversibility of aggregates and other associations can also be assessed

Although many biotech products are successfully stored in the frozen state, there are cases of degradation of biologicals during freeze storage. The degradation (e.g., aggregation) has been often linked to crystallization of a cryoprotector or pH changes while other factors include protein crowding and unfolding (either due to cold denaturation, interaction of protein molecules with ice crystals or air bubbles formed on the ice crystallization front) and mechanical stresses.

In this talk, I will discuss the latest developments in rational strategies to evaluate the effects of surface-mediated stress on protein stability. The focus will be on early detection and mechanistic understanding that will enable the creation of an effective control strategy in the industrial setting.

In this presentation, we will discuss strategies to enhance oral peptide bioavailability. This includes understanding the impact of peptide properties on oral absorption in the presence of permeation enhancers, as well as the effect of delivery site. Combining peptide engineering for oral delivery and formulation optimization for site-specific delivery can improve oral bioavailability. Additionally, we will present the controlled gastric delivery of a GIP/GLP-1 peptide in monkeys using mucoadhesive SNAC tablets.

Widespread use of peptide drugs like Ozempic raises concerns about the immunogenicity risks posed by generic versions. This presentation introduces orthogonal immunogenicity risk assessment methods for generic peptide drug impurities under the FDA’s Abbreviated New Drug Application (ANDA) pathway, focusing on two case studies: salmon calcitonin and teriparatide, to illustrate that understanding the inherent immunogenicity of the active pharmaceutical ingredient (API) is critical to estimating the potential immunogenicity of impurities.

Our work focuses on biointelligent biomaterial platforms that overcome the intrinsic barriers limiting peptide therapeutics.I will discuss how enzyme-responsive nanoparticles and hydrogels sense and respond to diseased microenvironments—stabilizing fragile peptides, navigating mucus and epithelial barriers, and localizing therapy with precision. These adaptive systems enable sustained delivery in the lung, mucosa, and osteoarthritic joints, opening new possibilities for clinically transformative peptide medicines.

MA-[D-Leu-4]-OB3 is a synthetic peptide leptin mimetic encompassing the functional epitope of the leptin molecule and engineered for optimal pharmacokinetics, efficacy, and oral or nasal administration. In mouse models of obesity, diabetes, and cognitive impairment, MA-[D-Leu-4]-OB3 has been shown to be safe and to have therapeutic and prophylactic efficacy. MA-[D-Leu-4]-OB3 reduces body weight gain, enhances insulin sensitivity, normalizes blood glucose, reverses diabetic dyslipidemia, promotes bone turnover, and enhances memory/cognition. Its ability to cross the blood-brain barrier, inhibit neuroinflammation and neurodegeneration, prevent/reduce beta-amyloid build-up, and improve cognitive function promises significant therapeutic benefit for an aging world population.