The Co-existence of the Gastrocnemius Tertius and Accessory Soleus Muscles

A bilateral gastrocnemius tertius muscle and a unilateral accessory soleus muscle were encountered during the routine educational dissection studies. The right gastrocnemius tertius muscle consisted of one belly, but the left one of two bellies. On the left side, the superficial belly of the gastrocnemius tertius muscle had its origin from an area just above the tendon of the plantaris muscle, the deep belly from the tendon of the plantaris muscle. The accessory soleus muscle originated from the posteromedial aspect of the tibia and soleal line of the tibia and inserted to the medial surface of the calcaneus. On the right side, the gastrocnemius tertius muscle had its origin from the lateral condyle of the femur, and inserted to the medial head of the gastrocnemius muscle. The co-existence of both gastrocnemius tertius and accessory soleus muscle has not, to our knowledge, been previously reported

Probing the surface chemistry of self-assembled peptide hydrogels using solution-state NMR spectroscopy

The surface chemistry of self-assembled hydrogel fibres – their charge, hydrophobicity and ion-binding dynamics – is recognised to play an important role in determining how the gels develop as well as their suitability for different applications. However, to date there are no established methodologies for the study of this surface chemistry. Here, we demonstrate how solution-state NMR spectroscopy can be employed to measure the surface chemical properties of the fibres in a range of hydrogels formed from N-functionalised dipeptides, an effective and versatile class of gelator that has attracted much attention. By studying the interactions with the gel fibres of a diverse range of probe molecules and ions, we can simultaneously study a number of surface chemical properties of the NMR invisible fibres in an essentially non-invasive manner. Our results yield fresh insights into the materials. Most notably, gel fibres assembled using different tiggering methods bear differing amounts of negative charge as a result of a partial deprotonation of the carboxylic acid groups of the gelators. We also demonstrate how chemical shift imaging (CSI) techniques can be applied to follow the formation of hydrogels along chemical gradients. We apply CSI to study the binding of Ca2+ and subsequent gelation of peptide assemblies at alkaline pH. Using metal ion-binding molecules as probes, we are able to detect the presence of bound Ca2+ ions on the surface of the gel fibres. We briefly explore how knowledge of the surface chemical properties of hydrogels could be used to inform their practical application in fields such as drug delivery and environmental remediation