CloChat: Understanding How People Customize, Interact, and Experience Personas in Large Language Models

Large language models (LLMs) have facilitated significant strides in generating conversational agents, enabling seamless, contextually relevant dialogues across diverse topics. However, the existing LLM-driven conversational agents have fixed personalities and functionalities, limiting their adaptability to individual user needs. Creating personalized agent personas with distinct expertise or traits can address this issue. Nonetheless, we lack knowledge of how people customize and interact with agent personas. In this research, we investigated how users customize agent personas and their impact on interaction quality, diversity, and dynamics. To this end, we developed CloChat, an interface supporting easy and accurate customization of agent personas in LLMs. We conducted a study comparing how participants interact with CloChat and ChatGPT. The results indicate that participants formed emotional bonds with the customized agents, engaged in more dynamic dialogues, and showed interest in sustaining interactions. These findings contribute to design implications for future systems with conversational agents using LLMs.Comment: In Proceedings of the SIGCHI Conference on Human Factors in Computing Systems (CHI '24

Antifungal Activity and Action Mechanism of Histatin 5-Halocidin Hybrid Peptides against Candida ssp.

The candidacidal activity of histatin 5 is initiated through cell wall binding, followed by translocation and intracellular targeting, while the halocidin peptide exerts its activity by attacking the Candida cell membrane. To improve antimicrobial activities and to understand the killing mechanism of two peptides, six hybrid peptides were designed by conjugating histatin 5 and halocidin. A comparative approach was established to study the activity, salt tolerance, cell wall glucan binding assay, cytotoxicity, generation of ROS and killing kinetics. CD spectrometry was conducted to evaluate secondary structures of these hybrid peptides. Furthermore the cellular localization of hybrid peptides was investigated by confocal fluorescence microscopy. Of the six hybrid congeners, di-PH2, di-WP2 and HHP1 had stronger activities than other hybrid peptides against all tested Candida strains. The MIC values of these peptides were 1-2, 2-4 and 2-4 μg/ml, respectively. Moreover, none of the hybrid peptides was cytotoxic in the hemolytic assay and cell-based cytotoxicity assay. Confocal laser microscopy showed that di-PH2 and HHP1 were translocated into cytoplasm whereas di-WP2 was accumulated on surface of C. albicans to exert their candidacidal activity. All translocated peptides (Hst 5, P113, di-PH2) were capable of generating intracellular ROS except HHP1. Additionally, the KFH residues at C-terminal end of these peptides were assumed for core sequence for active translocation

Hemolytic activities of Hst5, P113, di-18Hc, Halocidin-P113 hybrid peptides and control peptide.

<p>1% of triton-X100 was used as the control for 100% hemolysis and 0.01% acetic acid was used as the peptide-free control. Percent hemolysis was calculated with the following equation: Hemolysis (%) = (A₅₄₀ of sample—A₅₄₀ of peptide-free control) / (A₅₄₀ of 100% control—A₅₄₀ of peptide-free control) × 100.</p

Killing kinetics of Hst5, P113, di-18Hc, hybrid peptides against <i>Candida albicans</i>.

<p>Killing kinetics of peptides against <i>C</i>. <i>albicans</i> was measured by colony count assay. Candida cells were treated with a different concentration of peptides at a determined time. 10 mM NaPB was used as a control. Killing percent was calculated with the following equation: Killing % = (number of control cell—number of treated cell)/control cell × 100.</p

CD spectra of Hst5, P113, di-18Hc and hybrid peptides.

<p>This study was performed with one concentration (200 μg/ml) of each peptide in various buffers: 10 mM sodium phosphate buffer (Red line), 50% TFE in phosphate buffer (green line) and 20 mg of laminarin in phosphate buffer.</p

Effects of salt on MICs of Hst 5, P113, di-18Hc and hybrid peptides against Candida strains.

<p>Effects of salt on MICs of Hst 5, P113, di-18Hc and hybrid peptides against Candida strains.</p

Amino acid sequence of histatin 5, halocidin and hybrid peptides.

<p>Amino acid sequence of histatin 5, halocidin and hybrid peptides.</p

The effects of azide on killing activity of peptides.

<p>Candida cells were pre-incubated with 10 mM NaPB containing 5 mM NaN₃ at 30°C for 60 min then washed prior to addition of F-peptides. F-Hst 5, F-P113, F-HHP1 and F-di-PH2 showed (A) reduced levels of cytosolic uptake and (B) killing activity in azide (NaN₃, 5 mM) treated cells, whereas F-di-WP2 and F-di-18Hc showed equivalent amounts of cell wall binding to azide-treated cells and killing activity as untreated controls.</p

The percentage of secondary structure of Hst5, P113, hybrid peptides and di-18Hc.

<p>The percentage of secondary structure of Hst5, P113, hybrid peptides and di-18Hc.</p

Effect of Lithium Bis(oxalato) borate Additive on Electrochemical Performance of Li1.17Ni0.17Mn0.5Co0.17O2 Cathodes for Lithium-Ion Batteries

Lithium bis(oxalato) borate (LiBOB) is utilized as an oxidative additive to prevent the unwanted electrolyte decomposition on the surface of Li1.17Ni0.17Mn0.5Co0.17O2 cathodes. Our investigation reveals that the LiBOB additive forms a protective layer on the cathode surface and effectively mitigates severe oxidative decomposition of LiPF6-based electrolytes. Noticeable improvements in the cycling stability and rate capability of Li1.17Ni0.17Mn0.5Co0.17O2 cathodes are achieved in the LiBOB-added electrolyte. After 100 cycles at 60 degrees C, the discharge capacity retention of the Li1.17Ni0.17Mn0.5Co0.17O2 cathode was 28.6% in the reference electrolyte, whereas the LiBOB-containing electrolyte maintained 77.6% of its initial discharge capacity. Moreover, the Li1.17Ni0.17Mn0.5Co0.17O2 cathode with LiBOB additive delivered a superior discharge capacity of 115 mAh g(-1) at a high rate of 2 C compared with the reference electrolyte. The OCV of a full cell charged in the reference electrolyte drastically decreased from 4.22 V to 3.52 V during storage at 60 degrees C, whereas a full cell charged in the LiBOB-added electrolyte exhibited superior retention of the OCV.close6